PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26950406-3 2016 In this study, replica exchange molecular dynamics simulations have been performed to elucidate for the first time the molecular mechanism of adsorption and subsequent unfolding of hen egg white lysozyme at low pH at a polarized 1,2-dichloroethane/water interface. Water 248-253 lysozyme Homo sapiens 195-203 26950406-6 2016 By contrast, as expected, lysozyme in neat water at low pH does not exhibit significant structural changes. Water 43-48 lysozyme Homo sapiens 26-34 26424533-0 2016 Unit cell structure of water-filled monoolein in inverted hexagonal mesophase in the presence of incorporated tricaprylin and entrapped lysozyme. Water 23-28 lysozyme Homo sapiens 136-144 26411334-0 2015 Spectroscopic and Microscopic Studies of Aggregation and Fibrillation of Lysozyme in Water/Ethanol Solutions. Water 85-90 lysozyme Homo sapiens 73-81 26411334-1 2015 The thermal aggregation of lysozyme has been analyzed in water/ethanol solutions at low pH to induce the specific protein aggregation pathway which leads to fibrillar structures in a few hours. Water 57-62 lysozyme Homo sapiens 27-35 26002002-5 2015 Contact lens materials that have high ionicity and high water content have an increased affinity to accumulate lysozyme during wear, when compared with other soft lens materials, notably silicone hydrogel lenses. Water 56-61 lysozyme Homo sapiens 111-119 32261784-2 2014 The PNIPAM-b-LCP/SDS-functionalized 5CB droplets were effective in detecting proteins in water through a radial-to-bipolar (R-B) orientational change, with detection limits of 0.95, 1.1, 0.12, and 0.07 muM for bovine serum albumin (BSA), lysozyme (LYZ), hemoglobin (Hb), and chymotrypsinogen (ChTg), respectively. Water 89-94 lysozyme Homo sapiens 238-246 25525817-1 2015 We present a study of the interaction of the positively charged model protein lysozyme with the negatively charged amphiphilic diblock polyelectrolyte micelles of poly(tert-butylstyrene-b-sodium (sulfamate/carboxylate)isoprene) (PtBS-b-SCPI) on the silver/water interface. Water 256-261 lysozyme Homo sapiens 78-86 24969505-0 2014 Linear and nonlinear microrheology of lysozyme layers forming at the air-water interface. Water 73-78 lysozyme Homo sapiens 38-46 24969505-1 2014 We report experiments studying the mechanical evolution of layers of the protein lysozyme adsorbing at the air-water interface using passive and active microrheology techniques to investigate the linear and nonlinear rheological response, respectively. Water 111-116 lysozyme Homo sapiens 81-89 25156670-1 2014 Lysozyme can be electrochemically detected after adsorption at an electrified gel-water interface. Water 82-87 lysozyme Homo sapiens 0-8 32261784-2 2014 The PNIPAM-b-LCP/SDS-functionalized 5CB droplets were effective in detecting proteins in water through a radial-to-bipolar (R-B) orientational change, with detection limits of 0.95, 1.1, 0.12, and 0.07 muM for bovine serum albumin (BSA), lysozyme (LYZ), hemoglobin (Hb), and chymotrypsinogen (ChTg), respectively. Water 89-94 lysozyme Homo sapiens 248-251 24929414-4 2014 The use of heavy water and partly deuterated trehalose gives clear information on protein-trehalose interactions in the native state of lysozyme (at room temperature) and during the thermal denaturation process of lysozyme. Water 17-22 lysozyme Homo sapiens 136-144 24929414-4 2014 The use of heavy water and partly deuterated trehalose gives clear information on protein-trehalose interactions in the native state of lysozyme (at room temperature) and during the thermal denaturation process of lysozyme. Water 17-22 lysozyme Homo sapiens 214-222 23011876-6 2013 Moreover, our study reveals that the structural, dynamical, and vibrational properties of the hydration water of lysozyme are less sensitive to pressure than those of bulk water, thereby evidencing the strong influence of the protein surface on hydration water. Water 104-109 lysozyme Homo sapiens 113-121 26819974-1 2014 Recent studies have outlined the use of eutectic solutions of lithium chloride in water to study microscopic dynamics of lysozyme in an aqueous solvent that is remarkably similar to pure water in many respects, yet allows experiments over a wide temperature range without solvent crystallization. Water 82-87 lysozyme Homo sapiens 121-129 24655207-0 2014 Effect of ethanol-water mixture on the structure and dynamics of lysozyme: a fluorescence correlation spectroscopy study. Water 18-23 lysozyme Homo sapiens 65-73 24655207-1 2014 Effect of ethanol-water mixture on the hydrodynamic radius (r(H)) and conformational dynamics of lysozyme has been studied by circular dichroism, emission spectra, and fluorescence correlation spectroscopy. Water 18-23 lysozyme Homo sapiens 97-105 24291767-4 2014 The experimental approach consists in studying FTIR spectra of intrinsic chromophores and VT-NMR measurements on lysozyme water mixtures in the presence of trehalose. Water 122-127 lysozyme Homo sapiens 113-121 24121352-3 2013 A globular protein, lysozyme, adsorbed at the air-water interface is found to unfold into a flat shape within 1 s. Water 50-55 lysozyme Homo sapiens 20-28 28811453-1 2013 Lysozyme (LSZ)-loaded poly-L-lactide (PLLA) porous microparticles (PMs) were successfully prepared by a compressed CO2 antisolvent process in combination with a water-in-oil emulsion process using LSZ as a drug model and ammonium bicarbonate as a porogen. Water 161-166 lysozyme Homo sapiens 0-8 28811453-1 2013 Lysozyme (LSZ)-loaded poly-L-lactide (PLLA) porous microparticles (PMs) were successfully prepared by a compressed CO2 antisolvent process in combination with a water-in-oil emulsion process using LSZ as a drug model and ammonium bicarbonate as a porogen. Water 161-166 lysozyme Homo sapiens 10-13 23237985-2 2013 Using lysozyme as a cationic model protein these water soluble polymers efficiently self-assemble into nanocomplexes by charge attraction. Water 49-54 lysozyme Homo sapiens 6-14 23402521-3 2013 Complete deuteration effects on amidic groups were revealed through the analysis of the amide I band of lysozyme dissolved in deuterated water. Water 137-142 lysozyme Homo sapiens 104-112 23404569-0 2013 The effect of complex solvents on the structure and dynamics of protein solutions: The case of Lysozyme in trehalose/water mixtures. Water 117-122 lysozyme Homo sapiens 95-103 23968114-1 2013 The aim of this study is to simultaneously monitor the excess partial Gibbs energies, enthalpies, and entropies of water and white egg lysozyme and demonstrate how these quantities correlate with the coverage of the protein macromolecules by water molecules. Water 242-247 lysozyme Homo sapiens 135-143 23557185-2 2013 In this study, Raman spectroscopy was used to probe the hydration induced structural changes at various sites of lysozyme under isothermal conditions in the range of water contents from 0 to 44 wt %. Water 166-171 lysozyme Homo sapiens 113-121 23557185-9 2013 The native structure of lysozyme was achieved at 35 wt % water where its content is high enough for filling the space between lysozyme molecules. Water 57-62 lysozyme Homo sapiens 24-32 23557185-9 2013 The native structure of lysozyme was achieved at 35 wt % water where its content is high enough for filling the space between lysozyme molecules. Water 57-62 lysozyme Homo sapiens 126-134 23384517-3 2013 When an initial flux of 25 L/m(2)h was applied, both flux reduction and foulant mass deposition were severe for feed water containing the mixture of LYS and ALG (e.g., 50% LYS and 50% ALG at a total foulant concentration of 100 mg/L). Water 117-122 lysozyme Homo sapiens 149-152 23011876-6 2013 Moreover, our study reveals that the structural, dynamical, and vibrational properties of the hydration water of lysozyme are less sensitive to pressure than those of bulk water, thereby evidencing the strong influence of the protein surface on hydration water. Water 172-177 lysozyme Homo sapiens 113-121 23011876-6 2013 Moreover, our study reveals that the structural, dynamical, and vibrational properties of the hydration water of lysozyme are less sensitive to pressure than those of bulk water, thereby evidencing the strong influence of the protein surface on hydration water. Water 172-177 lysozyme Homo sapiens 113-121 23295480-7 2013 This study revealed successful lysozyme phasing by SAD using laboratory-source data involving Eu ions, which are mainly coordinated by the side chains of Asn46, Asp52 and Asp101 together with some water molecules. Water 197-202 lysozyme Homo sapiens 31-39 23093378-7 2012 Moreover, based on the difference in intermolecular distances distribution of water molecules (obtained from spectral data), we demonstrated that the lysozyme molecule causes a decrease in population of weak hydrogen bonds, and concurrently increases the probability of an occurrence of short hydrogen bonds in water affected by lysozyme. Water 78-83 lysozyme Homo sapiens 329-337 23390573-1 2013 In order to investigate the cryoprotective mechanism of trehalose on proteins, we use molecular dynamics computer simulations to study the microscopic dynamics of water upon cooling in an aqueous solution of lysozyme and trehalose. Water 163-168 lysozyme Homo sapiens 208-216 23390573-3 2013 Comparing aqueous solutions of lysozyme with/without trehalose, we observe that the dynamics of water in the hydration layers close to the protein is dramatically slower when trehalose is present in the system. Water 96-101 lysozyme Homo sapiens 31-39 23390573-4 2013 We also analyze the structure of water and trehalose around the lysozyme and find that the trehalose molecules form a cage surrounding the protein that contains very slow water molecules. Water 33-38 lysozyme Homo sapiens 64-72 23390573-4 2013 We also analyze the structure of water and trehalose around the lysozyme and find that the trehalose molecules form a cage surrounding the protein that contains very slow water molecules. Water 171-176 lysozyme Homo sapiens 64-72 23093378-0 2012 Characteristics of hydration water around hen egg lysozyme as the protein model in aqueous solution. Water 29-34 lysozyme Homo sapiens 50-58 23093378-4 2012 Analysis of spectra of HDO isotopically diluted in water solution of lysozyme allowed us to isolate HDO spectra affected by lysozyme, and thus to characterise the energetic state of water molecules and their arrangement around protein molecules. Water 51-56 lysozyme Homo sapiens 69-77 23093378-4 2012 Analysis of spectra of HDO isotopically diluted in water solution of lysozyme allowed us to isolate HDO spectra affected by lysozyme, and thus to characterise the energetic state of water molecules and their arrangement around protein molecules. Water 51-56 lysozyme Homo sapiens 124-132 23093378-7 2012 Moreover, based on the difference in intermolecular distances distribution of water molecules (obtained from spectral data), we demonstrated that the lysozyme molecule causes a decrease in population of weak hydrogen bonds, and concurrently increases the probability of an occurrence of short hydrogen bonds in water affected by lysozyme. Water 311-316 lysozyme Homo sapiens 150-158 23093378-4 2012 Analysis of spectra of HDO isotopically diluted in water solution of lysozyme allowed us to isolate HDO spectra affected by lysozyme, and thus to characterise the energetic state of water molecules and their arrangement around protein molecules. Water 182-187 lysozyme Homo sapiens 69-77 23093378-4 2012 Analysis of spectra of HDO isotopically diluted in water solution of lysozyme allowed us to isolate HDO spectra affected by lysozyme, and thus to characterise the energetic state of water molecules and their arrangement around protein molecules. Water 182-187 lysozyme Homo sapiens 124-132 23093378-7 2012 Moreover, based on the difference in intermolecular distances distribution of water molecules (obtained from spectral data), we demonstrated that the lysozyme molecule causes a decrease in population of weak hydrogen bonds, and concurrently increases the probability of an occurrence of short hydrogen bonds in water affected by lysozyme. Water 78-83 lysozyme Homo sapiens 150-158 23093378-7 2012 Moreover, based on the difference in intermolecular distances distribution of water molecules (obtained from spectral data), we demonstrated that the lysozyme molecule causes a decrease in population of weak hydrogen bonds, and concurrently increases the probability of an occurrence of short hydrogen bonds in water affected by lysozyme. Water 311-316 lysozyme Homo sapiens 329-337 22096116-8 2012 In a partitioned CAP, we found that when we added Lzm-S to a partitioned space in which a semipermeable membrane prevented diffusion of Lzm-S to the carotid artery tissue, vasodilation still occurred because of diffusion of H(2)O(2). Water 224-229 lysozyme Homo sapiens 50-53 22829567-0 2012 Behavior of lysozyme at the electrified water/room temperature ionic liquid interface. Water 40-45 lysozyme Homo sapiens 12-20 22829567-1 2012 Between the phases: The globular protein lysozyme was adsorbed and desorbed under electrochemical conditions at the water/room temperature ionic liquid microinterface array; the electrochemical desorption process provides a basis for protein detection at these interfaces. Water 116-121 lysozyme Homo sapiens 41-49 22894179-7 2012 Furthermore, at low contents (h = 0.075), water systematically stiffens the vibrational motions of lysozyme and trehalose, whereas it increases their MSDs on the nanosecond (ns) time scale. Water 42-47 lysozyme Homo sapiens 99-107 22894179-8 2012 This stems from the hydrogen bonds (HBs) that lysozyme and trehalose form with water, which, interestingly, are stronger than the ones they form with each other but which, nonetheless, relax faster on the ns time scale, given the larger mobility of water. Water 79-84 lysozyme Homo sapiens 46-54 22894179-8 2012 This stems from the hydrogen bonds (HBs) that lysozyme and trehalose form with water, which, interestingly, are stronger than the ones they form with each other but which, nonetheless, relax faster on the ns time scale, given the larger mobility of water. Water 249-254 lysozyme Homo sapiens 46-54 22894179-9 2012 Moreover, lysozyme interacts preferentially with water in the hydrated LT mixtures, and trehalose appears to slow down significantly the relaxation of lysozyme-water HBs. Water 49-54 lysozyme Homo sapiens 10-18 22894179-9 2012 Moreover, lysozyme interacts preferentially with water in the hydrated LT mixtures, and trehalose appears to slow down significantly the relaxation of lysozyme-water HBs. Water 160-165 lysozyme Homo sapiens 151-159 22882159-1 2012 In this work, we present a series of fully atomistic molecular dynamics (MD) simulations to study lysozyme"s orientation-dependent adsorption on polyethylene (PE) surface in explicit water. Water 183-188 lysozyme Homo sapiens 98-106 22115717-5 2012 SH-modified lysozyme showed largely unfolded structure in water and alpha-helical structure in the presence of ethanol. Water 58-63 lysozyme Homo sapiens 12-20 22998072-0 2012 Characteristic size for onset of coffee-ring effect in evaporating lysozyme-water solution droplets. Water 76-81 lysozyme Homo sapiens 67-75 22587099-6 2012 In turn, the case of the first hydration layers of the lysozyme molecule is shown to be more complicated, but still displaying signs of both kinds of behavior, together with a tendency of the proximal water molecules to hydrogen bond to the protein both as donors and as acceptors. Water 201-206 lysozyme Homo sapiens 55-63 21628092-0 2011 The influence of size, structure and hydrophilicity of model surfactants on the adsorption of lysozyme to oil-water interface--interfacial shear measurements. Water 110-115 lysozyme Homo sapiens 94-102 22712059-0 2012 Denaturation and aggregation of lysozyme in water-ethanol solution. Water 44-49 lysozyme Homo sapiens 32-40 22712059-5 2012 The rheological characteristics of lysozyme-water-ethanol solution changes from Newtonian to pseudoplastic. Water 44-49 lysozyme Homo sapiens 35-43 22001535-4 2011 Water was used as the solvent to solubilize lysozyme and thus no organic residual was detected. Water 0-5 lysozyme Homo sapiens 44-52 22225188-0 2011 Preferential solvation of lysozyme in water/ethanol mixtures. Water 38-43 lysozyme Homo sapiens 26-34 22225188-1 2011 We provide a quantitative description of the solvation properties of lysozyme in water/ethanol mixtures, which has been obtained by a simultaneous analysis of small-angle neutron scattering and differential scanning calorimetry experiments. Water 81-86 lysozyme Homo sapiens 69-77 21628092-7 2011 The adsorption of lysozyme to the oil-water interface results in the formation of a viscoelastic film. Water 38-43 lysozyme Homo sapiens 18-26 21628092-9 2011 The more hydrophilic surfactants are more effective in hindering lysozyme adsorption to oil-water interfaces. Water 92-97 lysozyme Homo sapiens 65-73 21641610-0 2011 How to obtain a well-spread monolayer of lysozyme at the air/water interfaces. Water 61-66 lysozyme Homo sapiens 41-49 21786812-4 2011 Using five of these mesogenic molecules as additives to induce protein crystallization, we discover that molecules that can form liquid crystal phases in water are highly effective at inducing the crystal formation of lysozyme, even at concentrations significantly lower than that required for forming liquid crystal phases. Water 154-159 lysozyme Homo sapiens 218-226 21506575-5 2011 Lysozyme was crystallized in-meso from three common LLC phases (lamellar, inverse hexagonal, and inverse bicontinuous cubic) composed of monolinolein and water. Water 154-159 lysozyme Homo sapiens 0-8 20104549-4 2010 Surface pressure versus area isotherms indicate that lysozyme is adsorbed by the surfactant-clay L-B film at the air-water interface without phase transition. Water 117-122 lysozyme Homo sapiens 53-61 20041676-6 2010 Further MD runs are carried out in explicit water for the native structure and the most stable adsorption state to assess the local stability of the geometry obtained in implicit solvent, and to calculate the statistical distribution of the water molecules around the whole lysozyme and its backbone. Water 241-246 lysozyme Homo sapiens 274-282 21428665-1 2011 We have performed an atomistic molecular dynamics simulation of an aqueous solution of hen egg-white lysozyme at room temperature with explicit water molecules. Water 144-149 lysozyme Homo sapiens 101-109 21517540-7 2011 Using nuclear magnetic resonance to measure the isotherms of lysozyme in situ between 18 and 2 C, the present work provides evidence that the part of water uptake associated with the onset of protein function is significantly reduced below 8 C. Quantitative analysis shows that such reduction is directly related to the reduction of protein flexibility and enhanced cost in elastic energy upon hydration at lower temperature. Water 151-156 lysozyme Homo sapiens 61-69 20676413-0 2010 Link between the hydration enthalpy of lysozyme and the density of its hydration water: Electrostriction. Water 81-86 lysozyme Homo sapiens 39-47 20676413-4 2010 The mean mass density of the hydration shell of lysozyme derived from the neutron and X-ray scattering is explained as following the compression of water in the fields of the order of 10(9) V m(-1) due to the charged sites at the boundary of the protein. Water 148-153 lysozyme Homo sapiens 48-56 20676413-5 2010 The mean enthalpy of mixing DeltaH(mean) of lysozyme in water calculated on the basis of the measured mean mass density falls in the middle of the values of the enthalpy of mixing DeltaH(mix) observed in sorption experiments. Water 56-61 lysozyme Homo sapiens 44-52 20586320-7 2010 At this step, the simulated environment of lysozyme was a water box, and the mica wafer was manually modeled according to its crystal structure. Water 58-63 lysozyme Homo sapiens 43-51 20197185-0 2010 Identification of salivary proteins at oil-water interfaces stabilized by lysozyme and beta-lactoglobulin. Water 43-48 lysozyme Homo sapiens 74-82 19555082-0 2009 Micro-Raman spectroscopic observation of water expulsion induced destruction of hydrophobic clusters in crystalline lysozyme. Water 41-46 lysozyme Homo sapiens 116-124 20059115-8 2009 Finally, the Raman susceptibility of sugar/water solutions and the calculated VDOS of water in the different lysozyme solutions confirm that sugars induce a significant strengthening of the hydrogen bond network of water that may stabilize proteins at high temperatures. Water 86-91 lysozyme Homo sapiens 109-117 19924849-1 2009 Photon correlation spectroscopy and circular dichroism have been used to study the role of hydration in the structure and thermostability of the model protein lysozyme in water-glycerol mixtures. Water 171-176 lysozyme Homo sapiens 159-167 19746957-2 2009 Specifically, we have measured the nine multicomponent diffusion coefficients, D(ij), for the lysozyme-poly(ethylene glycol)-NaCl-water system at pH 4.5 and 25 degrees C using precision Rayleigh interferometry. Water 130-135 lysozyme Homo sapiens 94-102 19353641-1 2009 2SS[6-127,64-80] variant of lysozyme which has two disulfide bridges, Cys6-Cys127 and Cys64-Cys80, and lacks the other two disulfide bridges, Cys30-Cys115 and Cys76-Cys94, was quite unstructured in water, but a part of the polypeptide chain was gradually frozen into a native-like conformation with increasing glycerol concentration. Water 198-203 lysozyme Homo sapiens 28-36 20059115-7 2009 These results suggest that sugars stiffen the environment experienced by lysozyme atoms, thereby counteracting the softening of protein vibrational modes upon denaturation, observed at high temperature in the Raman susceptibility of the lysozyme/water solution and in the computed VDOS of unfolded lysozyme in water. Water 246-251 lysozyme Homo sapiens 73-81 20059115-7 2009 These results suggest that sugars stiffen the environment experienced by lysozyme atoms, thereby counteracting the softening of protein vibrational modes upon denaturation, observed at high temperature in the Raman susceptibility of the lysozyme/water solution and in the computed VDOS of unfolded lysozyme in water. Water 246-251 lysozyme Homo sapiens 237-245 20059115-7 2009 These results suggest that sugars stiffen the environment experienced by lysozyme atoms, thereby counteracting the softening of protein vibrational modes upon denaturation, observed at high temperature in the Raman susceptibility of the lysozyme/water solution and in the computed VDOS of unfolded lysozyme in water. Water 246-251 lysozyme Homo sapiens 237-245 20059115-7 2009 These results suggest that sugars stiffen the environment experienced by lysozyme atoms, thereby counteracting the softening of protein vibrational modes upon denaturation, observed at high temperature in the Raman susceptibility of the lysozyme/water solution and in the computed VDOS of unfolded lysozyme in water. Water 310-315 lysozyme Homo sapiens 73-81 20059115-8 2009 Finally, the Raman susceptibility of sugar/water solutions and the calculated VDOS of water in the different lysozyme solutions confirm that sugars induce a significant strengthening of the hydrogen bond network of water that may stabilize proteins at high temperatures. Water 86-91 lysozyme Homo sapiens 109-117 19573978-1 2009 Thermal unfolding of ribonuclease A, lysozyme, and chymotrypsinogen A was analyzed as a multisite reaction of a protein molecule with water and solute molecules. Water 134-139 lysozyme Homo sapiens 37-45 19555082-1 2009 In this paper, three kinds of solid lysozyme samples with different water contents were investigated by confocal Raman spectroscopy. Water 68-73 lysozyme Homo sapiens 36-44 19555082-2 2009 For the rod-like lysozyme crystal with highest water content, a sudden decrease of the intensity ratio of the doublet at 1338 and 1360 cm(-1) was observed when the ambient relative humidity (RH) was lower than 86%, indicating the destruction of hydrophobic clusters of lysozyme induced by the expulsion of the hydration water from the crystal. Water 47-52 lysozyme Homo sapiens 17-25 19555082-2 2009 For the rod-like lysozyme crystal with highest water content, a sudden decrease of the intensity ratio of the doublet at 1338 and 1360 cm(-1) was observed when the ambient relative humidity (RH) was lower than 86%, indicating the destruction of hydrophobic clusters of lysozyme induced by the expulsion of the hydration water from the crystal. Water 47-52 lysozyme Homo sapiens 269-277 19555082-2 2009 For the rod-like lysozyme crystal with highest water content, a sudden decrease of the intensity ratio of the doublet at 1338 and 1360 cm(-1) was observed when the ambient relative humidity (RH) was lower than 86%, indicating the destruction of hydrophobic clusters of lysozyme induced by the expulsion of the hydration water from the crystal. Water 320-325 lysozyme Homo sapiens 17-25 19446755-3 2009 The pegylated lysozyme/CyD polypseudorotaxanes were less soluble in water and the release rate of the pegylated protein decreased in the order of the pegylated lysozyme>the gamma-CyD polypseudorotaxane>the alpha-CyD polypseudorotaxane. Water 68-73 lysozyme Homo sapiens 14-22 18478369-0 2009 Adsorption behavior of lysozyme and Tween 80 at hydrophilic and hydrophobic silica-water interfaces. Water 83-88 lysozyme Homo sapiens 23-31 19450493-4 2009 Shearing of lysozyme in water altered the protein"s backbone structure, whereas similar shear rates in glycerol solution affected the solvent exposure of side-chain residues located toward the exterior of the lysozyme alpha-domain. Water 24-29 lysozyme Homo sapiens 12-20 18478369-3 2009 Here, we describe the interaction of the well-characterized, globular protein lysozyme with Tween 80 at solid-water interfaces. Water 110-115 lysozyme Homo sapiens 78-86 19044806-0 2008 Water in hydrated orthorhombic lysozyme crystal: Insight from atomistic simulations. Water 0-5 lysozyme Homo sapiens 31-39 19072146-0 2009 Driving force behind adsorption-induced protein unfolding: a time-resolved X-ray reflectivity study on lysozyme adsorbed at an air/water interface. Water 131-136 lysozyme Homo sapiens 103-111 18690732-1 2008 Molecular simulations were performed to study the interactions between a protein (lysozyme, LYZ) and phosphorylcholine-terminated self-assembled monolayers (PC-SAMs) in the presence of explicit water molecules and ions. Water 194-199 lysozyme Homo sapiens 82-90 18641079-3 2008 This finding is demonstrated by increases in the root mean-square deviations of the heavy atoms of lysozyme, in the solvent-accessible surface area of hydrophobic residues, and in the number of hydrogen bonds between lysozyme and water. Water 230-235 lysozyme Homo sapiens 217-225 18715021-2 2008 For this purpose, the adsorption of lysozyme at the hydrophilic silica-water interface has been chosen as a model system. Water 71-76 lysozyme Homo sapiens 36-44 19044806-1 2008 Biologically important water in orthorhombic lysozyme crystal is investigated using atomistic simulations. Water 23-28 lysozyme Homo sapiens 45-53 19044806-2 2008 A distinct hydration shell surrounding lysozyme molecules is found from the number distribution of water molecules. Water 99-104 lysozyme Homo sapiens 39-47 19044806-4 2008 Adsorption of water in the lysozyme crystal shows type-IV behavior. Water 14-19 lysozyme Homo sapiens 27-35 18616315-0 2008 Effect of the air-water interface on the structure of lysozyme in the presence of guanidinium chloride. Water 18-23 lysozyme Homo sapiens 54-62 18616315-1 2008 We report observations of the changes in the surface structure of lysozyme adsorbed at the air-water interface produced by the chemical denaturant guanidinium chloride. Water 95-100 lysozyme Homo sapiens 66-74 17574261-1 2007 In this paper, we studied the interaction between human unstimulated saliva and lysozyme-stabilized oil-in-water emulsions (10 wt/wt% oil phase, 10 mM NaCl, pH 6.7), to reveal the driving force for flocculation of these emulsions. Water 107-112 lysozyme Homo sapiens 80-88 18302358-1 2008 Micellar solutions made of a fully fluorinated surfactant, LiPFN, form water-soluble complexes with lysozyme in a wide concentration range. Water 71-76 lysozyme Homo sapiens 100-108 17824692-1 2007 The three-dimensional distribution function theory of molecular liquids is applied to lysozyme in mixtures of water and noble gases. Water 110-115 lysozyme Homo sapiens 86-94 18647045-0 2008 Microcalorimetric study of thermal unfolding of lysozyme in water/glycerol mixtures: an analysis by solvent exchange model. Water 60-65 lysozyme Homo sapiens 48-56 18647045-2 2008 In particular, the thermal denaturation of a model system formed by lysozyme dissolved in water in the presence of the stabilizing cosolvent glycerol has been considered. Water 90-95 lysozyme Homo sapiens 68-76 18289663-7 2008 Comparison of adsorption to ion-exchange resins and neutral ODS leads to the conclusion that the apparent standard free-energy of adsorption Delta Gads( degrees ) of Lys, HSA, and IgG is not large in comparison to thermal energy due to energy-compensating interactions between water, protein, and ion-exchange surfaces that leaves a small net Delta Gads( degrees ). Water 277-282 lysozyme Homo sapiens 166-169 18446279-4 2008 As a practical example, a full simulation of the protein lysozyme in water is described step by step, including examples of necessary hardware and software, how to obtain suitable starting molecular structures, immersing it in a solvent, choosing good simulation parameters, and energy minimization. Water 69-74 lysozyme Homo sapiens 57-65 17574261-2 2007 Confocal scanning laser microscopy (CSLM) showed formation of complexes between salivary proteins and lysozyme adsorbed at the oil-water interface and lysozyme in solution as well. Water 131-136 lysozyme Homo sapiens 102-110 17014133-0 2006 Mechanical properties of interfacial films formed by lysozyme self-assembly at the air-water interface. Water 87-92 lysozyme Homo sapiens 53-61 17672727-0 2007 Role of the solvent in the dynamical transitions of proteins: the case of the lysozyme-water system. Water 87-92 lysozyme Homo sapiens 78-86 17672727-1 2007 We study the dynamics of hydration water in the protein lysozyme in the temperature range 180 K<T<360 K using Fourier-transform-infrared and nuclear magnetic resonance (NMR) spectroscopies. Water 35-40 lysozyme Homo sapiens 56-64 17600444-0 2007 Preferential hydration of lysozyme in water/glycerol mixtures: a small-angle neutron scattering study. Water 38-43 lysozyme Homo sapiens 26-34 17600444-1 2007 In solution small-angle neutron scattering has been used to study the solvation properties of lysozyme dissolved in water/glycerol mixtures. Water 116-121 lysozyme Homo sapiens 94-102 16802304-1 2006 The gelation process of lysozyme in water/tetramethylurea in the presence of salt was investigated as a function of temperature and system composition by rheology, infrared spectroscopy, and microcalorimetry. Water 36-41 lysozyme Homo sapiens 24-32 17125398-0 2006 Collective dynamics of lysozyme in water: terahertz absorption spectroscopy and comparison with theory. Water 35-40 lysozyme Homo sapiens 23-31 16870505-4 2007 Analysis of experimental data on intramolecular radioactivity distribution in lysozyme and computer simulation of tritium bombardment allowed us to suggest two equally probable opposite orientations of lysozyme molecule in the adsorption layer at the air-water interface. Water 255-260 lysozyme Homo sapiens 202-210 17014133-1 2006 We present the first characterization of the mechanical properties of lysozyme films formed by self-assembly at the air-water interface using the Cambridge interfacial tensiometer (CIT), an apparatus capable of subjecting protein films to a much higher level of extensional strain than traditional dilatational techniques. Water 120-125 lysozyme Homo sapiens 70-78 17014133-4 2006 We have also identified a previously undescribed pH dependency in the effect of solution ionic strength on the mechanical strength of the lysozyme films formed at the air-water interface. Water 171-176 lysozyme Homo sapiens 138-146 16706476-5 2006 At higher water contents, however, the denatured lysozyme can absorb a greater amount of water than the native protein due to the larger number of available sorption sites. Water 10-15 lysozyme Homo sapiens 49-57 16898772-1 2006 We report the four diffusion coefficients for the lysozyme-MgCl2-water ternary system at 25 degrees C and pH 4.5. Water 65-70 lysozyme Homo sapiens 50-58 16898772-2 2006 The comparison with previous results for the lysozyme-NaCl-water ternary system is used to examine the effect of salt stoichiometry on the transport properties of lysozyme-salt aqueous mixtures. Water 59-64 lysozyme Homo sapiens 163-171 16706476-5 2006 At higher water contents, however, the denatured lysozyme can absorb a greater amount of water than the native protein due to the larger number of available sorption sites. Water 89-94 lysozyme Homo sapiens 49-57 16706476-7 2006 Despite the unfolded structure, the denatured lysozyme binds less water than does the native lysozyme in the desorption experiments at water contents up to 34 wt %. Water 66-71 lysozyme Homo sapiens 46-54 16706476-7 2006 Despite the unfolded structure, the denatured lysozyme binds less water than does the native lysozyme in the desorption experiments at water contents up to 34 wt %. Water 135-140 lysozyme Homo sapiens 46-54 16706476-7 2006 Despite the unfolded structure, the denatured lysozyme binds less water than does the native lysozyme in the desorption experiments at water contents up to 34 wt %. Water 135-140 lysozyme Homo sapiens 93-101 16084007-1 2005 The effects of spin state of water molecules on its absorption on lyophilized DNA, lysozyme and some inorganic sorbents were studied. Water 29-34 lysozyme Homo sapiens 83-91 15089713-3 2004 Monte Carlo simulations and calculations show that this can be explained by the confinement of lysozyme molecules to the narrow water cells in the cubic phase. Water 128-133 lysozyme Homo sapiens 95-103 16309259-2 2005 Recent small-angle X-ray and neutron scattering data indicate that the density of water on the surface of lysozyme is significantly higher than in bulk water. Water 82-87 lysozyme Homo sapiens 106-114 16309259-2 2005 Recent small-angle X-ray and neutron scattering data indicate that the density of water on the surface of lysozyme is significantly higher than in bulk water. Water 152-157 lysozyme Homo sapiens 106-114 15858274-0 2005 Water molecules in the antibody-antigen interface of the structure of the Fab HyHEL-5-lysozyme complex at 1.7 A resolution: comparison with results from isothermal titration calorimetry. Water 0-5 lysozyme Homo sapiens 86-94 15858274-5 2005 The refined structure has yielded a detailed picture of the Fab-lysozyme interface, showing the high complementarity of the protein surfaces as well as several water molecules within the interface that complete the good fit. Water 160-165 lysozyme Homo sapiens 64-72 15207533-7 2004 The results in this study suggested that lysozyme, processed by freeze-drying, is stabilised primarily by the water substitution mechanism. Water 110-115 lysozyme Homo sapiens 41-49 16239747-2 2005 This article, by computing these lysozyme crystals" atomic structures, obtained by the diffraction patterns of microfocused synchrotron radiation, provides a possible mechanism for this increased stability, namely a significant decrease in water content accompanied by a minor but significant alpha-helix increase. Water 240-245 lysozyme Homo sapiens 33-41 15935361-1 2005 In this work, the gelation kinetics and fractal character of lysozyme gel matrices developed in tetramethylurea (TMU)-water media were investigated. Water 118-123 lysozyme Homo sapiens 61-69 16042464-1 2005 The effect of pH on the adsorption of catalase and lysozyme at the air-water interface has been studied using a combined surface pressure-interfacial shear rheology technique. Water 71-76 lysozyme Homo sapiens 51-59 16852340-2 2005 We show in detail how the spanning (percolating) water network appears at the surfaces of model hydrophilic spheres and at the surface of a single protein (lysozyme) molecule. Water 49-54 lysozyme Homo sapiens 156-164 16019886-8 2005 While the primary emulsion was stirred without quenching, lysozyme in the inner water phase continued diffusing across the ethyl acetate phase into the aqueous continuous phase. Water 80-85 lysozyme Homo sapiens 58-66 16019886-9 2005 Emulsion droplets were also broken into smaller ones with ongoing stirring; this event also contributed to lysozyme leaking out of the inner water phase. Water 141-146 lysozyme Homo sapiens 107-115 14663547-11 2004 The same is true for comparison between water and water-acetic acid for folded cyt c and Lyz. Water 40-45 lysozyme Homo sapiens 89-92 15801450-0 2004 Lysozyme adsorption studies at the silica/water interface using dual polarization interferometry. Water 42-47 lysozyme Homo sapiens 0-8 15801450-1 2004 Lysozyme adsorption at the silica/water interface has been studied using a new analytical technique called dual polarization interferometry. Water 34-39 lysozyme Homo sapiens 0-8 14663547-11 2004 The same is true for comparison between water and water-acetic acid for folded cyt c and Lyz. Water 50-55 lysozyme Homo sapiens 89-92 14518967-0 2003 Ovalbumin, ovotransferrin, lysozyme: three model proteins for structural modifications at the air-water interface. Water 98-103 lysozyme Homo sapiens 27-35 14518967-1 2003 Structural modifications of ovalbumin, ovotransferrin, and lysozyme at the air-water interface have been investigated using SDS-PAGE, both intrinsic and ANS fluorometry, and circular dichroism experiments. Water 79-84 lysozyme Homo sapiens 59-67 12659192-1 2003 Near pH 2.0, lysozyme in water is in its native conformation, and in water/methanol (2/8) it adopts a helical denatured conformation (Kamatari et al. Water 25-30 lysozyme Homo sapiens 13-21 12695708-1 2003 PURPOSE: To determine lysozyme deposition as a function of time in soft, high-water content, ionic (group IV) contact lenses. Water 78-83 lysozyme Homo sapiens 22-30 12957584-0 2003 Structure and denaturation of adsorbed lysozyme at the air-water interface. Water 59-64 lysozyme Homo sapiens 39-47 12659192-4 2003 Hydrogen/deuterium (H/D) exchange of lysozyme in solution confirms that it is partially unfolded at pH 2.0 in water/methanol (v/v = 2/8). Water 110-115 lysozyme Homo sapiens 37-45 12659192-5 2003 With electrospray ionization (ESI) mass spectrometry (MS), lysozyme in water produces ions with charges +7 to +12, with the greatest intensity at +10, whereas lysozyme in water/methanol (2/8) produces ions with charges +6 to +12 with the greatest intensity at +7. Water 71-76 lysozyme Homo sapiens 59-67 12659192-5 2003 With electrospray ionization (ESI) mass spectrometry (MS), lysozyme in water produces ions with charges +7 to +12, with the greatest intensity at +10, whereas lysozyme in water/methanol (2/8) produces ions with charges +6 to +12 with the greatest intensity at +7. Water 171-176 lysozyme Homo sapiens 159-167 12659192-11 2003 Thus, disulfide-intact gaseous lysozyme ions generated from the denatured state in water/methanol (2/8) refold into compact structures in the gas phase on a time scale of milliseconds or less. Water 83-88 lysozyme Homo sapiens 31-39 12214315-0 2002 Hydration structure of human lysozyme investigated by molecular dynamics simulation and cryogenic X-ray crystal structure analyses: on the correlation between crystal water sites, solvent density, and solvent dipole. Water 167-172 lysozyme Homo sapiens 29-37 12675337-3 2003 Through water injection, luminol and periodate were eluted from the anion-exchange column to generate the chemiluminescence, which was inhibited in the presence of lysozyme. Water 8-13 lysozyme Homo sapiens 164-172 12202382-0 2002 A model for water motion in crystals of lysozyme based on an incoherent quasielastic neutron-scattering study. Water 12-17 lysozyme Homo sapiens 40-48 12202382-1 2002 This paper reports an incoherent quasielastic neutron scattering study of the single particle, diffusive motions of water molecules surrounding a globular protein, the hen egg-white lysozyme. Water 116-121 lysozyme Homo sapiens 182-190 12202382-5 2002 The very good agreement between the structural and dynamical studies suggested a model for the dynamics of water in triclinic crystals of lysozyme in the time range approximately 330 ps and at 300 K. Herein, the dynamics of all water molecules is affected by the presence of the protein, and the water molecules can be divided into two populations. Water 107-112 lysozyme Homo sapiens 138-146 12202382-5 2002 The very good agreement between the structural and dynamical studies suggested a model for the dynamics of water in triclinic crystals of lysozyme in the time range approximately 330 ps and at 300 K. Herein, the dynamics of all water molecules is affected by the presence of the protein, and the water molecules can be divided into two populations. Water 228-233 lysozyme Homo sapiens 138-146 12202382-5 2002 The very good agreement between the structural and dynamical studies suggested a model for the dynamics of water in triclinic crystals of lysozyme in the time range approximately 330 ps and at 300 K. Herein, the dynamics of all water molecules is affected by the presence of the protein, and the water molecules can be divided into two populations. Water 228-233 lysozyme Homo sapiens 138-146 11959992-0 2002 Is the first hydration shell of lysozyme of higher density than bulk water? Water 69-74 lysozyme Homo sapiens 32-40 12124295-1 2002 We performed an elastic neutron scattering investigation of the molecular dynamics of lysozyme solvated in glycerol, at different water contents h (grams of water/grams of lysozyme). Water 130-135 lysozyme Homo sapiens 86-94 12124295-1 2002 We performed an elastic neutron scattering investigation of the molecular dynamics of lysozyme solvated in glycerol, at different water contents h (grams of water/grams of lysozyme). Water 157-162 lysozyme Homo sapiens 86-94 12124295-7 2002 This hydration-dependent dynamical activation, which is similar to that of hydrated lysozyme powders, is related to the specific interplay of the protein with the surrounding water and glycerol molecules. Water 175-180 lysozyme Homo sapiens 84-92 12084507-1 2002 Lysozyme-loaded poly(ethylene glycol terephthalate)-poly(butylene terephthalate) (PEGT/PBT) films were prepared using a water-in-oil emulsification solvent evaporation method. Water 120-125 lysozyme Homo sapiens 0-8 11959992-2 2002 Here, using molecular dynamics simulation, we provide an explanation of recent x-ray and neutron solution scattering data that indicate that the density of water on the surface of lysozyme is significantly higher than that of bulk water. Water 156-161 lysozyme Homo sapiens 180-188 11959992-2 2002 Here, using molecular dynamics simulation, we provide an explanation of recent x-ray and neutron solution scattering data that indicate that the density of water on the surface of lysozyme is significantly higher than that of bulk water. Water 231-236 lysozyme Homo sapiens 180-188 11856832-7 2002 Flash-cooled triclinic crystals of lysozyme, which have a smaller water content than the tetragonal form, diffract to higher resolution with smaller mosaicities and exhibit pronounced ordered domain structure even before annealing. Water 66-71 lysozyme Homo sapiens 35-43 11807248-4 2002 In test calculations, excellent agreement with experiment is found between neutron and X-ray scattering profiles calculated from a molecular-dynamics simulation of lysozyme in water. Water 176-181 lysozyme Homo sapiens 164-172 10102286-3 1999 RESULTS: Binding of lysozyme to high-water-content, ionic contact lenses (etafilcon A and vifilcon A) was dominated by a penetration process. Water 37-42 lysozyme Homo sapiens 20-28 11735996-2 2001 We have investigated the dynamics of protons along chains of hydrogen-bonded water molecules adsorbed on the surface of the globular protein lysozyme. Water 77-82 lysozyme Homo sapiens 141-149 11735996-4 2001 We find that the relaxation time diverges at a singular hydration that coincides with the critical water content required to trigger lysozyme enzymatic activity. Water 99-104 lysozyme Homo sapiens 133-141 11578104-0 2001 Improved activity and stability of lysozyme at the water/CH2Cl2 interface: enzyme unfolding and aggregation and its prevention by polyols. Water 51-56 lysozyme Homo sapiens 35-43 11578104-3 2001 When lysozyme was exposed to a large water/CH2Cl2 interface achieved by homogenization, lysozyme aggregation occurred. Water 37-42 lysozyme Homo sapiens 5-13 11578104-3 2001 When lysozyme was exposed to a large water/CH2Cl2 interface achieved by homogenization, lysozyme aggregation occurred. Water 37-42 lysozyme Homo sapiens 88-96 11578104-6 2001 The observed loss in specific enzyme activity of soluble lysozyme was caused by the irreversible formation of an unfolded lysozyme species, which was found to be monomeric, and was able to leave the water/CH2Cl2 interface and accumulate in the aqueous phase. Water 199-204 lysozyme Homo sapiens 57-65 11578104-6 2001 The observed loss in specific enzyme activity of soluble lysozyme was caused by the irreversible formation of an unfolded lysozyme species, which was found to be monomeric, and was able to leave the water/CH2Cl2 interface and accumulate in the aqueous phase. Water 199-204 lysozyme Homo sapiens 122-130 11397633-0 2001 Rotational and translational dynamics of lysozyme in water-glycerol solution. Water 53-58 lysozyme Homo sapiens 41-49 11397633-2 2001 For this, we investigated the dynamical properties of lysozyme in mixtures water-glycerol by means of parallel measurements of photon correlation spectroscopy (PCS) and dielectric spectroscopy at radiofrequencies (DS). Water 75-80 lysozyme Homo sapiens 54-62 11397633-5 2001 In order to ascertain if this effect is present also in our sample, we performed PCS and DS measurements on lysozyme-water-glycerol solutions. Water 117-122 lysozyme Homo sapiens 108-116 11397633-9 2001 These results indicate that the diffusive behavior of lysozyme in the water-glycerol mixture is coherent with the Debye-Stokes-Einstein hydrodynamic model. Water 70-75 lysozyme Homo sapiens 54-62 11523091-4 2001 The data obtained with lysozyme allow detection of minor conformational changes upon glycerol addition to the native protein, and suggest that the protein structure in the presence of the additive is slightly compressed compared with its state in water. Water 247-252 lysozyme Homo sapiens 23-31 11053145-0 2000 Molecular dynamics of solid-state lysozyme as affected by glycerol and water: a neutron scattering study. Water 71-76 lysozyme Homo sapiens 34-42 11053145-8 2000 Upon the addition of glycerol or water, anharmonicity was recovered above a dynamic transition temperature (T(d)), which may contribute to the reduction of T(m) values for dehydrated lysozyme in the presence of glycerol. Water 33-38 lysozyme Homo sapiens 183-191 11053145-9 2000 The greatest degree of anharmonicity, as well as the lowest T(d), was observed for lysozyme solvated with water. Water 106-111 lysozyme Homo sapiens 83-91 10713206-0 2000 Influence of water activity and aqueous solvent ordering on enzyme kinetics of alcohol dehydrogenase, lysozyme, and beta-galactosidase. Water 13-18 lysozyme Homo sapiens 102-110 10713206-1 2000 Effects of the water activity (a(w)) and the solvent ordering, as determined by the activity coefficient of water, were investigated on the enzyme kinetics of alcohol dehydrogenase, lysozyme, and beta-galactosidase in various aqueous solutions. Water 15-20 lysozyme Homo sapiens 182-190 10713206-1 2000 Effects of the water activity (a(w)) and the solvent ordering, as determined by the activity coefficient of water, were investigated on the enzyme kinetics of alcohol dehydrogenase, lysozyme, and beta-galactosidase in various aqueous solutions. Water 108-113 lysozyme Homo sapiens 182-190 10667860-7 2000 However, Lyso reactivity reached a maximum when the concentration of micelles was approximately 1 x 10(-5), the same as the protein concentration In AOT reverse micelles, the quenching rate constants decreased > 75% with respect to water. Water 235-240 lysozyme Homo sapiens 9-13 11277716-2 2001 From a previous reported density function for lysozyme in water a simulated spectrum, without the superposition of statistical fluctuation and spectrometer resolution effects, was generated. Water 58-63 lysozyme Homo sapiens 46-54 11042546-0 2000 Phase equilibria in the lysozyme-ammonium sulfate-water system. Water 50-55 lysozyme Homo sapiens 24-32 10825558-4 2000 The efficiency of lysozyme entrapment by a double emulsion method was found to depend on the swelling behavior of the polymers in water and decreased from 100% for polymers with a degree of swelling of less than 1.8 to 11% for PEG-PBT copolymers with a degree of swelling of 3.6. Water 130-135 lysozyme Homo sapiens 18-26 9761646-1 1998 We have studied the adsorption of lysozyme layers at a hydrophobic silicon water interface using specular neutron reflection. Water 75-80 lysozyme Homo sapiens 34-42 9990012-1 1999 Hen egg-white lysozyme dissolved in glycerol containing 1% water was studied by using CD and amide proton exchange monitored by two-dimensional 1H NMR. Water 59-64 lysozyme Homo sapiens 14-22 9990012-2 1999 The far- and near-UV CD spectra of the protein showed that the secondary and tertiary structures of lysozyme in glycerol were similar to those in water. Water 146-151 lysozyme Homo sapiens 100-108 9990012-6 1999 The results point to a highly ordered, native-like structure of lysozyme in glycerol, with the stability exceeding that in water. Water 123-128 lysozyme Homo sapiens 64-72 9795050-1 1998 A new method for encapsulating a model protein, lysozyme into hydrophilic uncapped poly(d,l-lactic-co-glycolic acid) (PLGA) microspheres was developed using an oil/water (O/W) single emulsion technique. Water 164-169 lysozyme Homo sapiens 48-56 9717743-0 1998 Effect of Na+ and K+ ions on the initial crystallization process of lysozyme in the presence of D2O and H2O. Water 104-107 lysozyme Homo sapiens 68-76 9735207-7 1998 Globule-like macroions such as LZ and BSA show high surface activity at isoelectric point above m* accompanied with orientation of the molecules along the air-water interface. Water 159-164 lysozyme Homo sapiens 31-33 9717743-4 1998 The initial aggregation rate of lysozyme in H2O was slower than in D2O. Water 44-47 lysozyme Homo sapiens 32-40 9717743-2 1998 In the present studies, we examined the initial aggregation process of lysozyme (initial crystallization process of lysozyme) in D2O/H2O with sodium ions or potassium ions, and investigated the relationship between the surface hydrophobicity and the aggregation rate of lysozyme. Water 133-136 lysozyme Homo sapiens 71-79 9717743-7 1998 These results suggest that the interaction between lysozyme molecules is stronger in D2O than in H2O. Water 97-100 lysozyme Homo sapiens 51-59 9717743-2 1998 In the present studies, we examined the initial aggregation process of lysozyme (initial crystallization process of lysozyme) in D2O/H2O with sodium ions or potassium ions, and investigated the relationship between the surface hydrophobicity and the aggregation rate of lysozyme. Water 133-136 lysozyme Homo sapiens 116-124 9717743-2 1998 In the present studies, we examined the initial aggregation process of lysozyme (initial crystallization process of lysozyme) in D2O/H2O with sodium ions or potassium ions, and investigated the relationship between the surface hydrophobicity and the aggregation rate of lysozyme. Water 133-136 lysozyme Homo sapiens 116-124 9352681-6 1996 In the cases of cytochrome c and lysozyme, the water concentration was larger than that in the protein-free system in spite of the same AOT condition. Water 47-52 lysozyme Homo sapiens 33-41 9491923-6 1998 Lysozyme showed a critical concentration for nucleus formation whose value in H2O was lower than in D2O at 3% salt concentration. Water 78-81 lysozyme Homo sapiens 0-8 9491923-10 1998 Therefore, the effect of lysozyme concentration on the aggregation process in H2O may be smaller than in D2O. Water 78-81 lysozyme Homo sapiens 25-33 9333407-0 1997 [Water as a stabilizer and plasticizer of the globular structure of lysozyme]. Water 1-6 lysozyme Homo sapiens 68-76 9028884-0 1997 Surface Tension Kinetics of the Wild Type and Four Synthetic Stability Mutants of T4 Phage Lysozyme at the Air-Water Interface Surface tension kinetics exhibited by the wild type and selected stability mutants of T4 lysozyme at the air-water interface were monitored with DuNouy tensiometry. Water 111-116 lysozyme Homo sapiens 91-99 9022219-0 1996 Effects of distearoylphosphatidylglycerol and lysozyme on the structure of the monoolein-water cubic phase: X-ray diffraction and Raman scattering studies. Water 89-94 lysozyme Homo sapiens 11-54 8765133-11 1996 Temperature-induced phase separation was studied with EO30/PO70 at 45 degrees C. Both BSA and lysozyme were completely partitioned to the water phase formed above the cloud point of EO30/PO70. Water 138-143 lysozyme Homo sapiens 94-102 9659395-0 1998 X-ray studies on cross-linked lysozyme crystals in acetonitrile-water mixture. Water 64-69 lysozyme Homo sapiens 30-38 9512049-0 1998 Low-frequency Raman spectra of lysozyme crystals and oriented DNA films: dynamics of crystal water. Water 93-98 lysozyme Homo sapiens 31-39 9491923-0 1998 Kinetic studies on the initial crystallization process of lysozyme in the presence of D2O and H2O. Water 94-97 lysozyme Homo sapiens 58-66 9505202-4 1997 When the hydrogel complexed with lysozyme was placed in deionized water and various KCl solutions, of varying concentrations of up to 0.5 M KCl, no lysozyme was released in deionized water, while increasing amounts of lysozyme were released as the KCl concentration increased. Water 66-71 lysozyme Homo sapiens 33-41 9505202-4 1997 When the hydrogel complexed with lysozyme was placed in deionized water and various KCl solutions, of varying concentrations of up to 0.5 M KCl, no lysozyme was released in deionized water, while increasing amounts of lysozyme were released as the KCl concentration increased. Water 183-188 lysozyme Homo sapiens 33-41 8381363-2 1993 The H-D exchange reaction was initiated by transferring the lysozyme adsorbed on hydroxyapatite powder from H2O into D2O. Water 108-111 lysozyme Homo sapiens 60-68 15299307-1 1995 Studies on the low-humidity (88%) forms of tetragonal and monoclinic lysozyme, resulting from water-mediated transformations, have provided a wealth of information on the variability in protein hydration, its structural consequences and the water structure associated with proteins, in addition to facilitating the delineation of the rigid and the flexible regions in the protein molecule and the invariant features in its hydration shell. Water 94-99 lysozyme Homo sapiens 69-77 15299307-1 1995 Studies on the low-humidity (88%) forms of tetragonal and monoclinic lysozyme, resulting from water-mediated transformations, have provided a wealth of information on the variability in protein hydration, its structural consequences and the water structure associated with proteins, in addition to facilitating the delineation of the rigid and the flexible regions in the protein molecule and the invariant features in its hydration shell. Water 241-246 lysozyme Homo sapiens 69-77 8599674-1 1995 For hydrated metmyoglobin, methemoglobin, and lysozyme powders, the freezable water fraction of between approximately 0.3-0.4 g water/g protein up to approximately 0.7-0.8 g water/g protein has been fully vitrified by cooling at rates up to approximately 1500 K min-1 and the influence of cooling rate characterized by x-ray diffractograms. Water 78-83 lysozyme Homo sapiens 46-54 8599674-1 1995 For hydrated metmyoglobin, methemoglobin, and lysozyme powders, the freezable water fraction of between approximately 0.3-0.4 g water/g protein up to approximately 0.7-0.8 g water/g protein has been fully vitrified by cooling at rates up to approximately 1500 K min-1 and the influence of cooling rate characterized by x-ray diffractograms. Water 128-133 lysozyme Homo sapiens 46-54 8599674-1 1995 For hydrated metmyoglobin, methemoglobin, and lysozyme powders, the freezable water fraction of between approximately 0.3-0.4 g water/g protein up to approximately 0.7-0.8 g water/g protein has been fully vitrified by cooling at rates up to approximately 1500 K min-1 and the influence of cooling rate characterized by x-ray diffractograms. Water 128-133 lysozyme Homo sapiens 46-54 1447179-10 1992 Moreover, through the information of the tertiary structures of the apo- and holomutant lysozyme, it was confirmed that the entropy release (10 kcal/mol) upon the binding of Ca2+ arises primarily from the release of bound water molecules hydrating the free Ca2+. Water 222-227 lysozyme Homo sapiens 88-96 7679107-1 1993 Lysozyme and 10 other proteins are solubilized in reverse micelles formed by 0.1 M sodium di-2-ethyl-hexylsulfosuccinate and 2.0-2.5 M water (pH 7.4) in isooctane solvent. Water 135-140 lysozyme Homo sapiens 0-8 1381588-1 1992 Ozone is shown to react with lysozyme in reverse micelles formed by 0.1 M sodium di-2-ethylhexylsulfosuccinate and 1.2-3 M water (pH 7.4) in isooctane solvent. Water 123-128 lysozyme Homo sapiens 29-37 1819046-0 1991 Glycation of lysozyme in a restricted water environment. Water 38-43 lysozyme Homo sapiens 13-21 1911779-12 1991 We also discuss the effect of proline mutations on the energetics of the folding pathway of the h-lysozyme in water. Water 110-115 lysozyme Homo sapiens 98-106 1650249-1 1991 Protonic conduction studies are reported for lysozyme as a function of the number of bound water molecules. Water 91-96 lysozyme Homo sapiens 45-53 1931971-9 1991 These results can be seen to be consistent with UVCD and resolution-enhanced FTIR spectra of alpha-lactalbumin and lysozyme in both D2O and H2O environments. Water 140-143 lysozyme Homo sapiens 115-123 1819046-1 1991 Fast atom bombardment mass spectrometry (FAB) was used to determine the glycation sites of lysozyme in a restricted water environment. Water 116-121 lysozyme Homo sapiens 91-99 34619120-0 2022 Synthesis of gold nanoclusters-loaded lysozyme nanoparticles for ratiometric fluorescent detection of cyanide in tap water, cyanogenic glycoside-containing plants, and soils. Water 117-122 lysozyme Homo sapiens 38-46 1750738-4 1991 The mean tear lysozyme levels of rigid (1.12 +/- 0.54 g/L, P less than .05) and high water-content (1.20 +/- 0.43 g/L, P less than .03) contact lens wearers were increased in comparison with the control group. Water 85-90 lysozyme Homo sapiens 14-22 1750738-5 1991 The tear lysozyme difference was significant (P less than .03) between high and low water-content (0.82 +/- 0.20 g/L) contact lens users. Water 84-89 lysozyme Homo sapiens 9-17 1750738-7 1991 Contact lens wear is irritating to the cornea and conjunctiva, and tear lysozyme physiology is disturbed most by high water-content contact lenses. Water 118-123 lysozyme Homo sapiens 72-80 2207286-1 1990 13C-nmr spectra of lysozyme obtained at 50.3 MHz using both static and magic-angle-spinning-cross-polarization methods are reported at several water contents. Water 143-148 lysozyme Homo sapiens 19-27 2049821-1 1991 We used the heat denaturation of lysozyme to induce the in vitro formation of protein deposits on 60 poly-HEMA contact lenses (38.6% water). Water 133-138 lysozyme Homo sapiens 33-41 34635270-0 2022 A molecularly imprinted biosensor based on water-compatible and electroactive polymeric nanoparticles for lysozyme detection. Water 43-48 lysozyme Homo sapiens 106-114 34635270-1 2022 A molecularly imprinted biosensor for lysozyme based on the polymer nanoparticles self-assembled from water-soluble and electroactive poly (gamma-glutamic acid) modified with 3-aminothiophene copolymer were prepared. Water 102-107 lysozyme Homo sapiens 38-46 34635270-2 2022 The water-soluble copolymer made imprinting of lysozyme in aqueous solution possible and thus facilitated improvement of the activity of LYS. Water 4-9 lysozyme Homo sapiens 47-55 34917778-0 2021 The role of water in the reversibility of thermal denaturation of lysozyme in solid and liquid states. Water 12-17 lysozyme Homo sapiens 66-74 34917778-2 2021 We evaluated the reversibility of thermal unfolding of lysozyme with respect to the water content using a combination of thermodynamic and structural techniques such as differential scanning calorimetry, synchrotron small and wide-angle X-ray scattering (SWAXS) and Raman spectroscopy. Water 84-89 lysozyme Homo sapiens 55-63 34917778-7 2021 A phase diagram of thermal unfolding/denaturation in lysozyme - water system was constructed based on the experimental data. Water 64-69 lysozyme Homo sapiens 53-61 34685360-2 2021 A thermoresponsive polymer with upper critical solution temperature, poly(N-acryloyl glycinamide) (PNAGA), which is soluble in water at elevated temperatures but phase separates at low temperatures, has been shown to bind lysozyme, chosen as a model enzyme, at a low temperature (10 C and lower) but not at room temperature (around 25 C). Water 127-132 lysozyme Homo sapiens 222-230 34821675-7 2021 By changing the water saturation of the continuous phase, the equation of state of lysozyme in solution was determined through the relation of the osmotic pressure between protein molecules and the volume fraction of protein inside the droplets. Water 16-21 lysozyme Homo sapiens 83-91 34685367-1 2021 We combined broad-band depolarized light scattering and infrared spectroscopies to study the properties of hydration water in a lysozyme-trehalose aqueous solution, where trehalose is present above the concentration threshold (30% in weight) relevant for biopreservation. Water 117-122 lysozyme Homo sapiens 128-136 34265335-4 2021 Here, it is shown that insertion of small amounts of 4-(2-hydroxyethyl)-1-piperazineethanesulfonate (HEPES, 0.1 M) as a second additive to lysozyme-NaCl-water solutions near physiological ionic strength (0.2 M) is an essential step for triggering conversion of protein-rich droplets into another phase. Water 153-158 lysozyme Homo sapiens 139-147 34337627-1 2021 Introduction of the propyl-sulfonic acid group at N1 of the coordinated 2-(2-pyridyl)benzimidazole ligand (L) in (RhCl(eta5-C5Me5)L)(CF3SO3) gives rise to a water-soluble complex, which can bind to the model protein lysozyme via non-covalent interactions. Water 157-162 lysozyme Homo sapiens 216-224 34072871-5 2021 Here, we used the response surface methodology to optimize the production of COs by enzymatic hydrolysis of water-soluble chitin (WSC) with hen egg-white lysozyme. Water 108-113 lysozyme Homo sapiens 154-162 34170128-8 2021 All these results demonstrate lysozyme amyloid fibrils as an appropriate natural bio-flocculant for removing dispersed MPs, NOM, and turbid particles from water. Water 155-160 lysozyme Homo sapiens 30-38 34342225-3 2021 In the present study, we combine field-dependent NMR relaxation (NMRD) and theory to probe water dynamics on the surface of proteins in concentrated aqueous solutions of hen egg-white lysozyme (LZM) and bovine serum albumin (BSA). Water 91-96 lysozyme Homo sapiens 184-192 34342225-3 2021 In the present study, we combine field-dependent NMR relaxation (NMRD) and theory to probe water dynamics on the surface of proteins in concentrated aqueous solutions of hen egg-white lysozyme (LZM) and bovine serum albumin (BSA). Water 91-96 lysozyme Homo sapiens 194-197 34342225-4 2021 The experiments reveal that the presence of salts (NaCl or NaI) leads to an opposite ion-specific response for the two proteins: an addition of salt to LZM solutions increases water relaxation rates with respect to the salt-free case, while for BSA solutions, a decrease is observed. Water 176-181 lysozyme Homo sapiens 152-155 34179093-3 2021 The resulting multiscale decomposition of energy and entropy components for water, sodium chloride, excipients and lysozyme reveals that lysozyme is more stabilised by the interaction of tripolyphosphate with basic residues. Water 76-81 lysozyme Homo sapiens 137-145 35015542-8 2022 In the case of the hydrophobic amino acids in the protein lysozyme, the slow down in the thermal relaxation relative to that in water appears to be controlled primarily by the size of the side chain. Water 128-133 lysozyme Homo sapiens 58-66 35598422-5 2022 The studies on the interaction with two proteins, lysozyme (Lyz) chosen as a representative model of a small protein, and human serum albumin (HSA) show that two types of binding are possible: a non-covalent binding through the accessible residues on protein surface with (VIVO(L1-3)(LNN)) keeping its octahedral structure, and a covalent binding upon the replacement of water in (VIVO(L1-3)(H2O)) with His-N donors to form VIVO(L1-3)(HSA). Water 371-376 lysozyme Homo sapiens 50-58 35598422-5 2022 The studies on the interaction with two proteins, lysozyme (Lyz) chosen as a representative model of a small protein, and human serum albumin (HSA) show that two types of binding are possible: a non-covalent binding through the accessible residues on protein surface with (VIVO(L1-3)(LNN)) keeping its octahedral structure, and a covalent binding upon the replacement of water in (VIVO(L1-3)(H2O)) with His-N donors to form VIVO(L1-3)(HSA). Water 371-376 lysozyme Homo sapiens 60-63 35598422-5 2022 The studies on the interaction with two proteins, lysozyme (Lyz) chosen as a representative model of a small protein, and human serum albumin (HSA) show that two types of binding are possible: a non-covalent binding through the accessible residues on protein surface with (VIVO(L1-3)(LNN)) keeping its octahedral structure, and a covalent binding upon the replacement of water in (VIVO(L1-3)(H2O)) with His-N donors to form VIVO(L1-3)(HSA). Water 392-395 lysozyme Homo sapiens 50-58 35598422-5 2022 The studies on the interaction with two proteins, lysozyme (Lyz) chosen as a representative model of a small protein, and human serum albumin (HSA) show that two types of binding are possible: a non-covalent binding through the accessible residues on protein surface with (VIVO(L1-3)(LNN)) keeping its octahedral structure, and a covalent binding upon the replacement of water in (VIVO(L1-3)(H2O)) with His-N donors to form VIVO(L1-3)(HSA). Water 392-395 lysozyme Homo sapiens 60-63 35594491-0 2022 Gelation Dynamics upon Pressure-Induced Liquid-Liquid Phase Separation in a Water-Lysozyme Solution. Water 76-81 lysozyme Homo sapiens 82-90 35594491-1 2022 Employing X-ray photon correlation spectroscopy, we measure the kinetics and dynamics of a pressure-induced liquid-liquid phase separation (LLPS) in a water-lysozyme solution. Water 151-156 lysozyme Homo sapiens 157-165 35151821-2 2022 METHODS: Lysozyme/PHC mixtures with 1:1 and 1:3 (w/w) ratios are freeze-dried from either H2O or D2O solutions. Water 90-93 lysozyme Homo sapiens 9-17 35195865-6 2022 In comparison with raw sludge, adsorption water proportion in TB-EPS and S-EPS was reduced after lysozyme (LZM) or freezing-thaw conditioning, which was ascribed to reduction of EPS viscosity and the weakness of water adsorption capacity. Water 42-47 lysozyme Homo sapiens 97-105 35195865-6 2022 In comparison with raw sludge, adsorption water proportion in TB-EPS and S-EPS was reduced after lysozyme (LZM) or freezing-thaw conditioning, which was ascribed to reduction of EPS viscosity and the weakness of water adsorption capacity. Water 42-47 lysozyme Homo sapiens 107-110 35195865-6 2022 In comparison with raw sludge, adsorption water proportion in TB-EPS and S-EPS was reduced after lysozyme (LZM) or freezing-thaw conditioning, which was ascribed to reduction of EPS viscosity and the weakness of water adsorption capacity. Water 212-217 lysozyme Homo sapiens 97-105 35195865-6 2022 In comparison with raw sludge, adsorption water proportion in TB-EPS and S-EPS was reduced after lysozyme (LZM) or freezing-thaw conditioning, which was ascribed to reduction of EPS viscosity and the weakness of water adsorption capacity. Water 212-217 lysozyme Homo sapiens 107-110 35195865-10 2022 In addition, after LZM or freezing-thaw conditioning, the sludge particle size significantly increased after TB-EPS extraction, while the sludge particle more easily absorbed water molecules, thereby increasing adsorption water and capillary water within the sludge flocs. Water 175-180 lysozyme Homo sapiens 19-22 35195865-10 2022 In addition, after LZM or freezing-thaw conditioning, the sludge particle size significantly increased after TB-EPS extraction, while the sludge particle more easily absorbed water molecules, thereby increasing adsorption water and capillary water within the sludge flocs. Water 222-227 lysozyme Homo sapiens 19-22 35195865-10 2022 In addition, after LZM or freezing-thaw conditioning, the sludge particle size significantly increased after TB-EPS extraction, while the sludge particle more easily absorbed water molecules, thereby increasing adsorption water and capillary water within the sludge flocs. Water 242-247 lysozyme Homo sapiens 19-22 2765584-1 1989 Scanning calorimetry has been used for studying lysozyme water solutions of different buffer molarity (mu = 0.5 divided by 1.0) and concentrations (c = 1.5 divided by 25%) at pH 2.0. Water 57-62 lysozyme Homo sapiens 48-56 2611291-1 1989 Study of temperature dependence of heat capacity in denatured biopolymers (collagen, elastin, lysozyme, DNA) with 10-15% of bound water revealed a characteristic jump at some critical temperature Tc. Water 130-135 lysozyme Homo sapiens 94-102 7139045-1 1982 Nuclear magnetic relaxation measurements are reported as a function of field strength corresponding to the frequency range from 0.01 to 20 MHz for water protons in monoclinic lysozyme crystals at 278 and 298 K. Though the instrumentation used selects only a portion of the total magnetization to sample, the data clearly indicate a field dependence of the relaxation rate that signals the presence of slow motions characterized by time constants in the range of tenths of microseconds and slower. Water 147-152 lysozyme Homo sapiens 175-183 3421968-0 1988 Lysozyme kinetics in low water activity media. Water 25-30 lysozyme Homo sapiens 0-8 3421968-2 1988 The influence of water activity on initial lysozyme kinetics is studied. Water 17-22 lysozyme Homo sapiens 43-51 3421968-4 1988 This influence of water organization on initial enzyme activity is immediate and may be preserved even after a large dilution, thus lysozyme presents a "hydration memory" phenomenon. Water 18-23 lysozyme Homo sapiens 132-140 2423146-7 1986 Lysozyme is selectively adsorbed on all of the high water content hydrogels and mucin is the major protein component for the pure PHEMA type of lenses. Water 52-57 lysozyme Homo sapiens 0-8 17007768-1 1985 The solvophobic theory developed earlier by Sinanoglu introducing the use of molecular surface areas and microthermodynamic surface and interfacial tensions at molecular dimensions is applied to the interpretation of calorimetric data on denaturation of lysozyme in a wide range of methanol/water mixtures. Water 291-296 lysozyme Homo sapiens 254-262 3997320-2 1985 A water-soluble hydrocortisone complex also inhibited lysozyme release, but at high concentrations, lysis of the cells occurred. Water 2-7 lysozyme Homo sapiens 54-62 6699913-6 1984 For dried lysozyme (water content less than or equal to 0.5%, w/w) a nearly linear increase with frequency and an exponential increase with temperature of the absorption coefficient is observed between 50 K and 300 K. This frequency and temperature dependence is described by relaxation processes in asymmetric double-well potentials with relaxation times in the picosecond range. Water 20-25 lysozyme Homo sapiens 10-18 4426701-5 1974 Mature endosporulating spherules removed from growth medium and resuspended in a solution of human or HEW lysozyme at 18 mug/ml in distilled water prompted leakage of four to five times as much of materials absorbing maximally at 260 nm into the supernatant as untreated control spherules during 90 min of incubation. Water 141-146 lysozyme Homo sapiens 106-114 7436414-0 1980 Solvation of lysozyme in water/dioxane mixtures studied in the frozen state by NMR spectroscopy. Water 25-30 lysozyme Homo sapiens 13-21 427107-0 1979 Thermodynamics of the denaturation of lysozyme in alcohol--water mixtures. Water 59-64 lysozyme Homo sapiens 38-46 932018-3 1976 Sound velocities and heat capacities have also been measured for various concentrations of lysozyme-water solutions at 25 degrees. Water 100-105 lysozyme Homo sapiens 91-99 932018-6 1976 The number of water molecules hydrated to 1 mol of lysozyme was estimated from the volume and compressibility and found to be 162 at 25 degrees. Water 14-19 lysozyme Homo sapiens 51-59 4426701-6 1974 This four- to fivefold increase in nucleotide loss was evident at 4, 25, and 37 C. The permeability of 1-day-old immature spherules and 8-day-old endospores was considerably altered by lysozyme treatment of cells suspended in distilled water. Water 236-241 lysozyme Homo sapiens 185-193 7096284-0 1982 Calorimetric study on thermal denaturation of lysozyme in polyol-water mixtures. Water 65-70 lysozyme Homo sapiens 46-54 7192710-2 1981 Lysozyme solubilized in reverse micelles of bis(2-ethylhexyl) sodium sulfosuccinate in isooctane containing as little as 0.8% water (v/v) has been shown to be active. Water 126-131 lysozyme Homo sapiens 0-8 7192710-4 1981 The dependence of lysozyme activity on pH in reverse micelles is different than that in water, with the entire pH profile shifted 2 to 3 pH units higher in reverse micelles. Water 88-93 lysozyme Homo sapiens 18-26 7192710-7 1981 Spectroscopic studies (CD, fluorescence, and UV absorbance) indicate that the conformation of lysozyme is significantly different in reverse micelles compared to water. Water 162-167 lysozyme Homo sapiens 94-102 7192710-8 1981 In particular, CD studies indicate that the helical content of lysozyme changes from approximately 34% in water to approximately 48% in reverse micelles. Water 106-111 lysozyme Homo sapiens 63-71 444485-1 1979 Heat capacity of the lysozyme--water system. Water 31-36 lysozyme Homo sapiens 21-29 444485-2 1979 Calorimetric measurements of the heat capacity of the lysozyme-water system have been carried out over the full range of system composition at 25 degrees C. The partial specific heat capacity of the protein in dilute solution is 1.483 +/- 0.009 J K-1 g-1. Water 63-68 lysozyme Homo sapiens 54-62 444485-5 1979 The break in the heat capacity function at 0.38 h defines the amount of water needed to develop the equilibrium solution properties of lysozyme as being 300 molecules of water/protein molecule, just sufficient for monolayer coverage. Water 72-77 lysozyme Homo sapiens 135-143 444485-5 1979 The break in the heat capacity function at 0.38 h defines the amount of water needed to develop the equilibrium solution properties of lysozyme as being 300 molecules of water/protein molecule, just sufficient for monolayer coverage. Water 170-175 lysozyme Homo sapiens 135-143 5828-5 1976 Changing the solvent from water to D2O or by quenching experiments in presence of azide ions it could be shown that the desactivation of lysozyme is caused exclusively by singlet oxygen. Water 26-31 lysozyme Homo sapiens 137-145 240438-0 1975 Hydrogen ion titration of lysozyme in alcohol-water solutions. Water 46-51 lysozyme Homo sapiens 26-34 5668653-0 1968 Films of lysozyme adsorbed at air-water surfaces. Water 34-39 lysozyme Homo sapiens 9-17 5045096-0 1972 [Adsorption of water vapors by alpha-chymotrypsin and lysozyme]. Water 15-20 lysozyme Homo sapiens 54-62 5146570-1 1971 Comparative dilatometric study of acid-base reactions of lysozyme and ovalbumin in water and denaturing media. Water 83-88 lysozyme Homo sapiens 57-65 5769701-0 1969 Dielectric measurements of water sorbed on ovalbumin and lysozyme. Water 27-32 lysozyme Homo sapiens 57-65 32497668-1 2020 The influence of a wide spectrum of water-miscible organic cosolvents at different concentrations on the denaturation of hen egg-white lysozyme is studied using differential scanning calorimetry (DSC) and circular dichroism (CD). Water 36-41 lysozyme Homo sapiens 135-143 33346655-4 2020 The lysozyme structure was found to be partially folded in both reline and reline/water mixtures. Water 82-87 lysozyme Homo sapiens 4-12 33346655-5 2020 Root-mean-square deviation (RMSD) of the positions of Calpha atoms of lysozyme indicate that 50/50 reline/water solvent induces more destabilization in the conformation of HEWL than that by pure reline and 75/25 reline/water mixture. Water 106-111 lysozyme Homo sapiens 70-78 33346655-5 2020 Root-mean-square deviation (RMSD) of the positions of Calpha atoms of lysozyme indicate that 50/50 reline/water solvent induces more destabilization in the conformation of HEWL than that by pure reline and 75/25 reline/water mixture. Water 219-224 lysozyme Homo sapiens 70-78 33346655-6 2020 From the root-mean-square fluctuation (RMSF) analysis, it is found that the lysozyme active site (Glu35-Asp52) is quite stable in the presence of pure reline but it is least stable in the presence of 50/50 reline/water mixture. Water 213-218 lysozyme Homo sapiens 76-84 33317300-1 2020 We study, with molecular dynamics simulations, a lysozyme protein immersed in a water-trehalose solution upon cooling. Water 80-85 lysozyme Homo sapiens 49-57 33317300-3 2020 The alpha-relaxation shows a fragile to strong crossover about 20 higher than that in the bulk water phase and 15 higher than that in lysozyme hydration water without trehalose. Water 155-160 lysozyme Homo sapiens 136-144 34022315-3 2021 Inspired by the unique conformational behavior of lysozyme proteins in water-ethanol mixtures, we conducted quartz crystal microbalance-dissipation (QCM-D) and localized surface plasmon resonance (LSPR) measurements to systematically investigate the adsorption behavior of lysozyme proteins onto silica surfaces across a wide range of water-ethanol mixtures. Water 71-76 lysozyme Homo sapiens 50-58 34022315-4 2021 Our findings revealed that lysozyme adsorption behavior strongly depended on the ethanol fraction in a non-monotonic fashion and this trend could be rationalized by taking into account how competing effects of water and ethanol solvation influence solution-phase protein size and conformational stability. Water 210-215 lysozyme Homo sapiens 27-35 32721078-4 2021 We found that water molecules are held inside and on the surface of the Lys molecule, and the hydration structure around the tryptophan residue changes by photoexcitation. Water 14-19 lysozyme Homo sapiens 72-75 33525751-2 2021 This study aimed to link the structural analysis of adsorbed lysozyme at the water/gold surface at pH 7.5 in a wide range of concentrations. Water 77-82 lysozyme Homo sapiens 61-69 33211495-3 2020 Herein, we report lysozyme nanofilm composite membranes (LNCM) prepared by one-step methods with hydrophobic substrates at the air/water interface. Water 131-136 lysozyme Homo sapiens 18-26 33036320-1 2020 We report results on the translational dynamics of the hydration water of the lysozyme protein upon cooling obtained by means of molecular dynamics simulations. Water 65-70 lysozyme Homo sapiens 78-86 32585093-1 2020 In this study, the binding to lysozyme (Lyz) of four important VIV compounds with antidiabetic and/or anticancer activity, [VIVO(pic)2(H2O)], [VIVO(ma)2], [VIVO(dhp)2], and [VIVO(acac)2], where pic-, ma-, dhp-, and acac- are picolinate, maltolate, 1,2-dimethyl-3-hydroxy-4(1H)-pyridinonate, and acetylacetonate anions, and of the vanadium-containing natural product amavadin ([VIV(hidpa)2]2-, with hidpa3- N-hydroxyimino-2,2"-diisopropionate) was investigated by ElectroSpray Ionization-Mass Spectrometry (ESI-MS). Water 135-138 lysozyme Homo sapiens 30-38 32585093-1 2020 In this study, the binding to lysozyme (Lyz) of four important VIV compounds with antidiabetic and/or anticancer activity, [VIVO(pic)2(H2O)], [VIVO(ma)2], [VIVO(dhp)2], and [VIVO(acac)2], where pic-, ma-, dhp-, and acac- are picolinate, maltolate, 1,2-dimethyl-3-hydroxy-4(1H)-pyridinonate, and acetylacetonate anions, and of the vanadium-containing natural product amavadin ([VIV(hidpa)2]2-, with hidpa3- N-hydroxyimino-2,2"-diisopropionate) was investigated by ElectroSpray Ionization-Mass Spectrometry (ESI-MS). Water 135-138 lysozyme Homo sapiens 40-43 32585093-5 2020 The behavior of the systems with [VIVO(pic)2(H2O)] and Mb or Ub is very similar to that of Lyz. Water 45-48 lysozyme Homo sapiens 91-94 32432582-6 2020 Interestingly, the PEG-LZM-polyphenol hydrogel has a higher water content than other polyphenol-toughened hydrogels, which may better meet the clinical needs for hydrogel materials. Water 60-65 lysozyme Homo sapiens 23-26 32460500-3 2020 Our results demonstrated that the PA membrane surface"s roughness is a key factor of surface"s bio-fouling, as the lysozyme protein adsorbed on the surface"s cavity site displays extremely low surface diffusivity, blocking water passage and decreasing water flux. Water 223-228 lysozyme Homo sapiens 115-123 32460500-3 2020 Our results demonstrated that the PA membrane surface"s roughness is a key factor of surface"s bio-fouling, as the lysozyme protein adsorbed on the surface"s cavity site displays extremely low surface diffusivity, blocking water passage and decreasing water flux. Water 252-257 lysozyme Homo sapiens 115-123 31272172-1 2019 We use extended depolarized light scattering spectroscopy to study the dynamics of water in a lysozyme-trehalose aqueous solution over a broad time scale, from hundreds to fractions of picoseconds. Water 83-88 lysozyme Homo sapiens 94-102 32251594-0 2020 Structure Determination of Hen Egg-White Lysozyme Aggregates Adsorbed to Lipid/Water and Air/Water Interfaces. Water 79-84 lysozyme Homo sapiens 41-49 32251594-0 2020 Structure Determination of Hen Egg-White Lysozyme Aggregates Adsorbed to Lipid/Water and Air/Water Interfaces. Water 93-98 lysozyme Homo sapiens 41-49 31377191-0 2020 Dipole-dipole interactions between tryptophan side chains and hydration water molecules dominate the observed dynamic stokes shift of lysozyme. Water 72-77 lysozyme Homo sapiens 134-142 31377191-4 2020 To interpret the relaxation, a molecular dynamics simulation of 75 ns was conducted for lysozyme immersed in a water box. Water 111-116 lysozyme Homo sapiens 88-96 31377191-8 2020 In addition, by inspecting the variation in dipole moments of the hydration water molecules around lysozyme, it was suggested that the observed relaxation could be attributed to the orientational relaxation of hydration water molecules participating in the hydrogen-bond network formed around each of the two tryptophan residues. Water 76-81 lysozyme Homo sapiens 99-107 31377191-8 2020 In addition, by inspecting the variation in dipole moments of the hydration water molecules around lysozyme, it was suggested that the observed relaxation could be attributed to the orientational relaxation of hydration water molecules participating in the hydrogen-bond network formed around each of the two tryptophan residues. Water 220-225 lysozyme Homo sapiens 99-107 31272172-3 2019 By comparing aqueous solutions of lysozyme with and without trehalose, we show that the combined action of sugar and protein produces an exceptional dynamic slowdown of a fraction of water molecules around the protein, which become more than twice slower than in the absence of trehalose. Water 183-188 lysozyme Homo sapiens 34-42 31272172-6 2019 On the basis of these findings, we believe such ultraslow water close to the lysozyme is likely to be involved in the mechanism of bioprotection. Water 58-63 lysozyme Homo sapiens 77-85 29790558-4 2018 We show that lysozyme recognizes and disperses fullerene in water. Water 60-65 lysozyme Homo sapiens 13-21 29720354-10 2018 Lysozyme deposited on ionic, high water content lens materials such as etafilcon A show significantly higher surface and bulk activity than many other hydrogel lens materials. Water 34-39 lysozyme Homo sapiens 0-8 30052040-2 2018 The emission and circular dichroism data of protein depict the nonmonotonic change suggesting that the structure as well as local environment near the Trp of lysozyme modifies differently for different compositions of the ETH-water mixture. Water 226-231 lysozyme Homo sapiens 158-166 28937227-5 2017 I present here high-resolution elastic neutron scattering measurements of the atomistic dynamics of lysozyme in water. Water 112-117 lysozyme Homo sapiens 100-108 29658720-0 2018 Adsorption Behavior of Lysozyme at Titanium Oxide-Water Interfaces. Water 50-55 lysozyme Homo sapiens 23-31 29031849-0 2017 Investigation of factors affecting the stability of lysozyme spray dried from ethanol-water solutions. Water 86-91 lysozyme Homo sapiens 52-60 29031849-2 2017 In this study, lysozyme was chosen as a model pharmaceutical protein to study these aspects when spray drying from water-ethanol mixtures. Water 115-120 lysozyme Homo sapiens 15-23 29031849-6 2017 Fourier Transform Infrared (FTIR) and Circular Dichroism (CD) results showed that the native structures of lysozyme were largely restored upon reconstitution of the spray dried powder in water after the spray drying process. Water 187-192 lysozyme Homo sapiens 107-115 29031849-7 2017 This suggests that the bioactivity of lysozyme could be preserved adequately by optimization of both the formulation composition and process conditions even when spray drying from a water-ethanol mixture. Water 182-187 lysozyme Homo sapiens 38-46 29629770-0 2018 Adsorption of Denaturated Lysozyme at the Air-Water Interface: Structure and Morphology. Water 46-51 lysozyme Homo sapiens 26-34 29629770-1 2018 The application of protein deuteration and high flux neutron reflectometry has allowed a comparison of the adsorption properties of lysozyme at the air-water interface from dilute solutions in the absence and presence of high concentrations of two strong denaturants: urea and guanidine hydrochloride (GuHCl). Water 152-157 lysozyme Homo sapiens 132-140 29652825-7 2018 The results showed the lysozyme loaded composite gel had high porosity, excellent water absorption property, and good antimicrobial activities against Escherichia coli and Staphylococcus aureus. Water 82-87 lysozyme Homo sapiens 23-31 29166117-0 2017 Adsorption and conformations of lysozyme and alpha-lactalbumin at a water-octane interface. Water 68-73 lysozyme Homo sapiens 32-40 29166117-5 2017 In this paper, molecular dynamics simulations are used to investigate the adsorption and conformation of two similar proteins, lysozyme and alpha-lactalbumin, at a water-octane interface. Water 164-169 lysozyme Homo sapiens 127-135 28450247-7 2017 The hydrophobic properties of the CS films were increased by the addition of LY and REC, determined by water contact angle measurement. Water 103-108 lysozyme Homo sapiens 77-79 27318738-10 2016 Results showed that Ag/lyz-Mt nanomaterial could be a promising bactericide for water disinfection. Water 80-85 lysozyme Homo sapiens 23-26 28797927-0 2017 Molecular dynamics study of unfolding of lysozyme in water and its mixtures with dimethyl sulfoxide. Water 53-58 lysozyme Homo sapiens 41-49 28797927-1 2017 All-atom explicit solvent molecular dynamics was used to study the process of unfolding of hen egg white lysozyme in water and mixtures of water with dimethyl sulfoxide at different compositions. Water 117-122 lysozyme Homo sapiens 105-113 28695859-1 2017 Solutions of lysozyme in heavy water were studied by small-angle neutron scattering (SANS) at concentrations of 40, 20 and 10 mg ml-1 with and without the addition of precipitant, and at temperatures of 10, 20 and 30 C. In addition to the expected protein monomers, dimeric and octameric species were identified in solutions at the maximum concentration and close to the optimal conditions for crystallization. Water 31-36 lysozyme Homo sapiens 13-21 28576085-0 2017 Lysozyme in water-acetonitrile mixtures: Preferential solvation at the inner edge of excess hydration. Water 12-17 lysozyme Homo sapiens 0-8 28576085-4 2017 At high water content, the lysozyme has a higher affinity for water than for acetonitrile. Water 8-13 lysozyme Homo sapiens 27-35 28576085-4 2017 At high water content, the lysozyme has a higher affinity for water than for acetonitrile. Water 62-67 lysozyme Homo sapiens 27-35 28576085-6 2017 At the intermediate water content, the dehydrated lysozyme has a higher affinity for acetonitrile than for water. Water 20-25 lysozyme Homo sapiens 50-58 28576085-6 2017 At the intermediate water content, the dehydrated lysozyme has a higher affinity for acetonitrile than for water. Water 107-112 lysozyme Homo sapiens 50-58 28576085-8 2017 At the lowest water content, the organic solvent molecules are preferentially excluded from the dried lysozyme, resulting in the preferential hydration. Water 14-19 lysozyme Homo sapiens 102-110 28576085-11 2017 At high and intermediate water content, lysozyme is preferentially hydrated. Water 25-30 lysozyme Homo sapiens 40-48 28576085-13 2017 At low water content, the preferential binding of the acetonitrile molecules to the initially hydrated lysozyme was detected. Water 7-12 lysozyme Homo sapiens 103-111 28430436-1 2017 Here we reveal details of the interaction between human lysozyme proteins, both native and fibrils, and their water environment by intense terahertz time domain spectroscopy. Water 110-115 lysozyme Homo sapiens 56-64 28383588-3 2017 We measured the Im chi(2) spectra of hemoglobin, myoglobin, serum albumin and lysozyme at the air/water interface in the CH and OH stretching regions using heterodyne-detected vibrational sum frequency generation (HD-VSFG) spectroscopy, and we deduced the isoelectric point of the protein by monitoring the orientational flip-flop of water molecules at the interface. Water 98-103 lysozyme Homo sapiens 78-86 27620335-3 2016 Lysozyme was dissolved in solutions with various ratios of ethanol and water, and subsequently spray-dried. Water 71-76 lysozyme Homo sapiens 0-8 27620335-5 2016 The aerosol performance of the spray-dried lysozyme from ethanol-water solution was improved compared to that from pure water. Water 65-70 lysozyme Homo sapiens 43-51 27620335-5 2016 The aerosol performance of the spray-dried lysozyme from ethanol-water solution was improved compared to that from pure water. Water 120-125 lysozyme Homo sapiens 43-51 27620335-6 2016 The conformation of lysozyme in the ethanol-water solution and spray dried powder was altered, but the native structure of lysozyme was restored upon reconstitution in water after the spray drying process. Water 44-49 lysozyme Homo sapiens 20-28 27620335-6 2016 The conformation of lysozyme in the ethanol-water solution and spray dried powder was altered, but the native structure of lysozyme was restored upon reconstitution in water after the spray drying process. Water 168-173 lysozyme Homo sapiens 123-131 32264423-1 2017 C60@lysozyme showed significant visible light-induced singlet oxygen generation in water, indicating the potential of this hybrid as an agent for photodynamic therapy. Water 83-88 lysozyme Homo sapiens 0-12 28801577-7 2017 Upon removing the backbone connectivity by breaking all peptide bonds in lysozyme, we find that the hysteresis shifts towards the lower humidity regime, and the water uptake capacity is significantly enhanced. Water 161-166 lysozyme Homo sapiens 73-81 27973744-5 2017 The lowest detectable concentration for lysozyme was 0.5 mug/mL in water and 5 mug/mL on a stainless steel food-handling surface. Water 67-72 lysozyme Homo sapiens 40-48 27722290-0 2016 Activity and conformation of lysozyme in molecular solvents, protic ionic liquids (PILs) and salt-water systems. Water 98-103 lysozyme Homo sapiens 29-37 27575543-1 2016 Hofmeister anion effects on adsorption kinetics of the positively charged lysozyme (pH < pI) at an air-water interface were studied by surface tension measurements and time-resolved X-ray reflectometry. Water 106-111 lysozyme Homo sapiens 74-82 27575543-5 2016 In X-ray reflection studies, we observed that the lysozyme molecules initially adsorbed on the air-water interface have a flat unfolded structure as previously reported in the salt-free solution. Water 99-104 lysozyme Homo sapiens 50-58 27722290-8 2016 Due to the presence of a net surface charge on lysozyme, electrostatic interactions in PIL-water systems and salt solutions enhanced lysozyme activity more than the specific hydrogen-bond interactions present in non-ionic molecular solvents. Water 91-96 lysozyme Homo sapiens 47-55 27722290-8 2016 Due to the presence of a net surface charge on lysozyme, electrostatic interactions in PIL-water systems and salt solutions enhanced lysozyme activity more than the specific hydrogen-bond interactions present in non-ionic molecular solvents. Water 91-96 lysozyme Homo sapiens 133-141 27722290-11 2016 Preferential solvophobic effects along with bulky chemical structures were postulated to result in less competition with water at the specific hydration layer around the protein, thus reducing protein-solvent interactions and retaining lysozyme"s native conformation. Water 121-126 lysozyme Homo sapiens 236-244 27142255-4 2016 It was observed that these four hydrogels showed varied diffusion behavior for either negatively charged BSA or positively charged LYZ due to protein-polymer interaction and the free water content in hydrogel matrix. Water 183-188 lysozyme Homo sapiens 131-134 27372901-0 2016 Preferential solvation of lysozyme in dimethyl sulfoxide/water binary mixture probed by terahertz spectroscopy. Water 57-62 lysozyme Homo sapiens 26-34 27372901-1 2016 We report the changes in the hydration dynamics around a model protein hen egg white lysozyme (HEWL) in water-dimethyl sulfoxide (DMSO) binary mixture using THz time domain spectroscopy (TTDS) technique. Water 104-109 lysozyme Homo sapiens 85-93 27341101-5 2016 The water content controlled the appearance and intensity of the Raman band at ~1787 cm(-1) when lysozyme powders were thermally denatured at temperatures higher than Tm. Water 4-9 lysozyme Homo sapiens 97-105 27193313-0 2016 Salt effects on the picosecond dynamics of lysozyme hydration water investigated by terahertz time-domain spectroscopy and an insight into the Hofmeister series for protein stability and solubility. Water 62-67 lysozyme Homo sapiens 43-51 27193313-2 2016 We investigated the effects of Hofmeister salts on the picosecond dynamics of water around a lysozyme molecule using terahertz time-domain spectroscopy. Water 78-83 lysozyme Homo sapiens 93-101 27193313-4 2016 From the difference in the salt concentration dependence for various salts, it has been found that chaotropic anions make the dynamics of water around the lysozyme molecule slower, whereas kosmotropic anions make the dynamics faster. Water 138-143 lysozyme Homo sapiens 155-163 27193313-6 2016 This result indicates that the effects of anions on the dynamics of water around the lysozyme molecule are the opposite of those for bulk water. Water 68-73 lysozyme Homo sapiens 85-93 27193313-6 2016 This result indicates that the effects of anions on the dynamics of water around the lysozyme molecule are the opposite of those for bulk water. Water 138-143 lysozyme Homo sapiens 85-93