PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20857183-0 2010 Mechanism of gemini disulfide detergent mediated oxidative refolding of lysozyme in a new artificial chaperone system. Disulfides 20-29 lysozyme Homo sapiens 72-80 22948901-2 2012 In combination with m-nitrobenzyl alcohol, molecular ion charge states that are greater than the number of basic sites in the protein can be produced from these native solutions, even for lysozyme, which is conformationally constrained by four intramolecular disulfide bonds. Disulfides 259-268 lysozyme Homo sapiens 188-196 21911017-2 2011 Two novel linker molecules, containing an ester bond and/or a disulfide bond for temporary immobilization, were synthesized and conjugated to lysozyme. Disulfides 62-71 lysozyme Homo sapiens 142-150 21911017-7 2011 Upon hydrolysis of the ester bonds or incubation with glutathione to reduce disulfide bonds of the linker molecules that conjugate the lysozyme to the gel network, the modified lysozyme was mobilized and released from the hydrogel to the same extent as native lysozyme. Disulfides 76-85 lysozyme Homo sapiens 135-143 21911017-7 2011 Upon hydrolysis of the ester bonds or incubation with glutathione to reduce disulfide bonds of the linker molecules that conjugate the lysozyme to the gel network, the modified lysozyme was mobilized and released from the hydrogel to the same extent as native lysozyme. Disulfides 76-85 lysozyme Homo sapiens 177-185 21911017-7 2011 Upon hydrolysis of the ester bonds or incubation with glutathione to reduce disulfide bonds of the linker molecules that conjugate the lysozyme to the gel network, the modified lysozyme was mobilized and released from the hydrogel to the same extent as native lysozyme. Disulfides 76-85 lysozyme Homo sapiens 177-185 20857183-4 2010 Using lysozyme as a model protein we could demonstrate that the disulfide gemini detergents allow oxidative refolding of the protein in the absence of any external redox system in an "artificial chaperone system". Disulfides 64-73 lysozyme Homo sapiens 6-14 20857183-6 2010 The results point to an important role of the transiently formed mixed disulfides between the protein and the detergent (Prot-SS-Det) in the oxidative refolding process of lysozyme. Disulfides 71-81 lysozyme Homo sapiens 172-180 19353641-0 2009 Glycerol-induced folding of unstructured disulfide-deficient lysozyme into a native-like conformation. Disulfides 41-50 lysozyme Homo sapiens 61-69 19899791-6 2010 The changes in secondary structure and conformation of disulfide linkage (S-S) of lysozyme were investigated experimentally by circular dichroism analysis and micro-Raman spectra. Disulfides 55-64 lysozyme Homo sapiens 82-90 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. Disulfides 51-60 lysozyme Homo sapiens 28-36 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. Disulfides 123-132 lysozyme Homo sapiens 28-36 18710266-6 2008 The degree of cross-linking between lysozyme molecules was controlled by manipulating both the extent of chemical reduction of the intramolecular disulfide bonds and sonication time. Disulfides 146-155 lysozyme Homo sapiens 36-44 19449893-6 2009 LC-ESI-MS/MS and Western blotting analysis showed that lysozyme fragments were incorporated into the aggregates of ghost membrane proteins, which suggested that thio-disulfide exchange among lysozyme and membrane proteins was triggered when the fibrils interacted with erythrocyte membranes. Disulfides 166-175 lysozyme Homo sapiens 55-63 19449893-6 2009 LC-ESI-MS/MS and Western blotting analysis showed that lysozyme fragments were incorporated into the aggregates of ghost membrane proteins, which suggested that thio-disulfide exchange among lysozyme and membrane proteins was triggered when the fibrils interacted with erythrocyte membranes. Disulfides 166-175 lysozyme Homo sapiens 191-199 19449893-8 2009 The exposure of interior hydrophobic residues and the increased level of solvent-accessible disulfides in the lysozyme fibrils are thought to be involved in membrane disruption. Disulfides 92-102 lysozyme Homo sapiens 110-118 15122914-2 2004 We analyzed the extent of the formation of a disulfide bond in each lysozyme variant using a redox buffer (pH 8) containing 1.0 mM reduced and 0.1 mM oxidized glutathione in the absence or presence of 6 M guanidine hydrochloride. Disulfides 45-54 lysozyme Homo sapiens 68-76 17956144-3 2007 Unfolding of lysozyme structure was induced by PEF, accompanied by the cleavage of disulfide bonds and self-association aggregation when the applied PEF dosage was higher than a critical level. Disulfides 83-92 lysozyme Homo sapiens 13-21 16138305-0 2005 Characterisation of disulfide-bond dynamics in non-native states of lysozyme and its disulfide deletion mutants by NMR. Disulfides 20-29 lysozyme Homo sapiens 68-76 16138305-0 2005 Characterisation of disulfide-bond dynamics in non-native states of lysozyme and its disulfide deletion mutants by NMR. Disulfides 85-94 lysozyme Homo sapiens 68-76 16138305-1 2005 This report describes NMR-spectroscopic investigations of the conformational dynamics of disulfide bonds in hen-egg-white lysozyme substitution mutants. Disulfides 89-98 lysozyme Homo sapiens 122-130 16138305-3 2005 The NMR analysis of heteronuclear 15N-relaxation rates shows that the barrier to disulfide-bond isomerisation can vary substantially in different lysozyme mutants and depends on the residual structure present in these states. Disulfides 81-90 lysozyme Homo sapiens 146-154 16138305-4 2005 The investigations reveal cooperativity in the modulation of micro- to millisecond dynamics that is due to the presence of multiple disulfide bridges in lysozyme. Disulfides 132-141 lysozyme Homo sapiens 153-161 15907935-7 2005 The disulfide-deficient hen lysozyme offers a particularly simple model system for thermodynamic and kinetic studies of protofibril formation as well as for screening drugs for amyloidosis. Disulfides 4-13 lysozyme Homo sapiens 28-36 18072203-0 2007 Expression of proteins containing disulfide bonds in an insect cell-free system and confirmation of their arrangements by MALDI-TOF MS. Escherichia coli alkaline phosphatase (AP) and human lysozyme (h-LYZ), which contain two and four disulfide bonds, respectively, were expressed in a cell-free protein synthesis system constructed from Spodoptera frugiperda 21 (Sf21) cells. Disulfides 34-43 lysozyme Homo sapiens 189-204 17310324-6 2007 Hence, the renaturation of disulfide-containing lysozyme was highly affected by the extent of denaturation. Disulfides 27-36 lysozyme Homo sapiens 48-56 15122914-3 2004 In the presence of 6 M guanidine hydrochloride, the extent of the formation of the disulfide bond in each lysozyme variant was proportional to the distance between cysteine residues, indicating that reduced hen lysozyme under a highly denaturing condition adopted a randomly coiled structure. Disulfides 83-92 lysozyme Homo sapiens 106-114 15122914-3 2004 In the presence of 6 M guanidine hydrochloride, the extent of the formation of the disulfide bond in each lysozyme variant was proportional to the distance between cysteine residues, indicating that reduced hen lysozyme under a highly denaturing condition adopted a randomly coiled structure. Disulfides 83-92 lysozyme Homo sapiens 211-219 15122914-6 2004 Moreover, the scattering data for the extents of the formation of the disulfide bonds among all lysozyme variants were observed. Disulfides 70-79 lysozyme Homo sapiens 96-104 14741343-2 2004 Equilibrium intermediates of disulfide reduced lysozyme in TFE are known to contain considerable amounts of alpha-helical structure and resemble the early intermediate in the oxidative refolding of lysozyme. Disulfides 29-38 lysozyme Homo sapiens 47-55 15016916-2 2004 Here, we show that an intrinsically unfolded protein (U), represented by a disulfide-deficient variant of hen lysozyme with no tertiary structure, forms an amyloid-like fibril after prolonged incubation. Disulfides 75-84 lysozyme Homo sapiens 110-118 14741343-2 2004 Equilibrium intermediates of disulfide reduced lysozyme in TFE are known to contain considerable amounts of alpha-helical structure and resemble the early intermediate in the oxidative refolding of lysozyme. Disulfides 29-38 lysozyme Homo sapiens 198-206 12492154-1 2002 Aggregate formation and the structure of the aggregates of disulfide-reduced proteins were investigated using alpha-lactalbumin and lysozyme as model proteins. Disulfides 59-68 lysozyme Homo sapiens 132-140 15115177-3 2004 We demonstrate here such divergent folding mechanisms of lysozyme and alphaLA using the technique of disulfide scrambling. Disulfides 101-110 lysozyme Homo sapiens 57-65 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. Disulfides 6-15 lysozyme Homo sapiens 31-39 16233527-1 2003 A porous wool keratin sponge was used for immobilization of lysozyme, a model bioactive substance and was demonstrated to be a unique biomaterial in terms that the activity of lysozyme linked to the sponge through disulfide bond was gradually released, while lysozyme through thioether bond was stably maintained. Disulfides 214-223 lysozyme Homo sapiens 60-68 16233527-1 2003 A porous wool keratin sponge was used for immobilization of lysozyme, a model bioactive substance and was demonstrated to be a unique biomaterial in terms that the activity of lysozyme linked to the sponge through disulfide bond was gradually released, while lysozyme through thioether bond was stably maintained. Disulfides 214-223 lysozyme Homo sapiens 176-184 16233527-1 2003 A porous wool keratin sponge was used for immobilization of lysozyme, a model bioactive substance and was demonstrated to be a unique biomaterial in terms that the activity of lysozyme linked to the sponge through disulfide bond was gradually released, while lysozyme through thioether bond was stably maintained. Disulfides 214-223 lysozyme Homo sapiens 176-184 12052074-0 2002 High-pressure refolding of disulfide-cross-linked lysozyme aggregates: thermodynamics and optimization. Disulfides 27-36 lysozyme Homo sapiens 50-58 11340658-0 2001 Crystal structure of a mutant human lysozyme with a substituted disulfide bond. Disulfides 64-73 lysozyme Homo sapiens 36-44 11340658-1 2001 The three-dimensional structure of a mutant human lysozyme, W64CC65A, in which a non-native disulfide bond Cys64--Cys81 is substituted for the Cys65--Cys81 of the wild type protein by replacing Trp64 and Cys65 with Cys and Ala, respectively, was determined by X-ray crystallography and refined to an R-value of 0.181, using 33,187 reflections at 1.87-A resolution. Disulfides 92-101 lysozyme Homo sapiens 50-58 11134973-6 2001 Heterogeneous proteins become cross-linked following the formation of heteromolecular interchain disulfide bonds during thermal unfolding of a mixture of of ribonuclease A and lysozyme. Disulfides 97-106 lysozyme Homo sapiens 176-184 10356266-3 1999 The reduced lysozyme lacking disulfide bonds was found to have a property similar to that of the molten globule state in terms of its local hydrophobicity, which was determined with the aqueous two-phase partitioning method. Disulfides 30-39 lysozyme Homo sapiens 13-21 10727242-0 2000 Effect of an alternative disulfide bond on the structure, stability, and folding of human lysozyme. Disulfides 25-34 lysozyme Homo sapiens 90-98 10727242-1 2000 Human lysozyme has four disulfide bonds, one of which, Cys65-Cys81, is included in a long loop of the beta-domain. Disulfides 24-33 lysozyme Homo sapiens 6-14 10727242-3 2000 Here, using the W64CC65A mutant, we investigated the effects of an alternative disulfide bond on the structure, stability, and folding of human lysozyme using circular dichroism (CD) and fluorescence spectroscopy combined with a stopped-flow technique. Disulfides 79-88 lysozyme Homo sapiens 144-152 10727242-8 2000 The Gibbs" free-energy diagrams obtained from the kinetic analysis suggest that the structure around the loop region in the beta-domain of human lysozyme is formed after the transition state of folding, and thus, the effect of the alternative disulfide bond on the structure, stability, and folding of human lysozyme appears mainly in the native state. Disulfides 243-252 lysozyme Homo sapiens 145-153 10727242-8 2000 The Gibbs" free-energy diagrams obtained from the kinetic analysis suggest that the structure around the loop region in the beta-domain of human lysozyme is formed after the transition state of folding, and thus, the effect of the alternative disulfide bond on the structure, stability, and folding of human lysozyme appears mainly in the native state. Disulfides 243-252 lysozyme Homo sapiens 308-316 10356266-4 1999 The reduced lysozyme was more clearly retarded on the ILC column than the native and 1 M guanidinium hydrochloride (GuHCl)-treated lysozymes with intact disulfide bonds. Disulfides 154-163 lysozyme Homo sapiens 13-21 8663382-4 1996 However, refolding of denatured/reduced lysozyme into buffer that lacks thiol/disulfide reagents leads to aggregation. Disulfides 78-87 lysozyme Homo sapiens 40-48 1634546-0 1992 Folding of human lysozyme in vivo by the formation of an alternative disulfide bond. Disulfides 69-78 lysozyme Homo sapiens 17-25 8069219-0 1994 Native disulfide bonds greatly accelerate secondary structure formation in the folding of lysozyme. Disulfides 7-16 lysozyme Homo sapiens 90-98 8069219-2 1994 Within the first 4 ms of folding, lysozyme with intact disulfide bonds already had a far-UV CD spectrum reflecting large amounts of secondary structure. Disulfides 55-64 lysozyme Homo sapiens 34-42 8069219-4 1994 Thus, native disulfide bonds not only stabilize the cfinal conformation of lysozyme but also provide, in early folding intermediates, the necessary stabilization that favors the formation of secondary structure. Disulfides 13-22 lysozyme Homo sapiens 75-83 8344427-1 1993 A mutant human lysozyme, designated as C77A-a, in which glutathione is bound to Cys95, has been shown to mimic an intermediate in the formation of a disulfide bond during folding of human (h)-lysozyme. Disulfides 149-158 lysozyme Homo sapiens 15-23 8344427-1 1993 A mutant human lysozyme, designated as C77A-a, in which glutathione is bound to Cys95, has been shown to mimic an intermediate in the formation of a disulfide bond during folding of human (h)-lysozyme. Disulfides 149-158 lysozyme Homo sapiens 192-200 8344427-2 1993 Protein disulfide isomerase (PDI), which is believed to catalyze disulfide bond formation and associated protein folding in the endoplasmic reticulum, attacked the glutathionylated h-lysozyme C77A-a to dissociate the glutathione molecule. Disulfides 8-17 lysozyme Homo sapiens 183-191 1416967-3 1992 The results showed that during the beginning of renaturation almost all reduced and denatured lysozyme is converted to forms possessing lower compactness than native lysozyme, probably as a result of formation of only one or two disulfide bonds. Disulfides 229-238 lysozyme Homo sapiens 94-102 1416967-4 1992 Kinetic analysis of lysozyme during renaturation showed that the generation of lysozyme with four disulfide bonds was not necessarily equivalent to the formation lysozyme with native-like catalytic properties. Disulfides 98-107 lysozyme Homo sapiens 79-87 1416967-4 1992 Kinetic analysis of lysozyme during renaturation showed that the generation of lysozyme with four disulfide bonds was not necessarily equivalent to the formation lysozyme with native-like catalytic properties. Disulfides 98-107 lysozyme Homo sapiens 79-87 1416967-5 1992 It appeared that the formation rate of the structures of the structures of the substrate binding site and of the catalytic site were limited by the generation of four disulfide bonds containing lysozyme. Disulfides 167-176 lysozyme Homo sapiens 194-202 1525170-0 1992 Enthalpic destabilization of a mutant human lysozyme lacking a disulfide bridge between cysteine-77 and cysteine-95. Disulfides 63-72 lysozyme Homo sapiens 44-52 2040307-1 1991 To investigate the mechanism of disulfide-bond-coupled de novo folding of human lysozyme, we have constructed 23 mutant enzymes in which cysteine residue(s) were replaced by alanine(s). Disulfides 32-41 lysozyme Homo sapiens 80-88 2404763-6 1990 These observations, plus structural considerations, suggest that Cys77 and Cys95 either remain uncrosslinked or the disulfide bond Cys77-Cys95, once formed, is opened during the final step in the folding of human lysozyme in vivo. Disulfides 116-125 lysozyme Homo sapiens 213-221 2007594-0 1991 Evidence for intramolecular disulfide bond shuffling in the folding of mutant human lysozyme. Disulfides 28-37 lysozyme Homo sapiens 84-92 2007594-1 1991 Our previous results using the Saccharomyces cerevisiae secretion system suggest that intramolecular exchange of disulfide bonds occurs in the folding pathway of human lysozyme in vivo (Taniyama, Y., Yamamoto, Y., Kuroki, R., and Kikuchi, M. (1990) J. Biol. Disulfides 113-122 lysozyme Homo sapiens 168-176 2007594-14 1991 These results suggest that the introduction of Cys83 and Cys91 may act to suppress the process of native disulfide bond formation through disulfide bond interchange in the folding of human lysozyme. Disulfides 105-114 lysozyme Homo sapiens 189-197 2007594-14 1991 These results suggest that the introduction of Cys83 and Cys91 may act to suppress the process of native disulfide bond formation through disulfide bond interchange in the folding of human lysozyme. Disulfides 138-147 lysozyme Homo sapiens 189-197 1180968-15 1975 The two disulfides 64-80 and 76-94 bring these two parts of the lysozyme molecule into a single reactive site. Disulfides 8-18 lysozyme Homo sapiens 64-72 3288200-0 1988 Role of disulfide bonds in folding and secretion of human lysozyme in Saccharomyces cerevisiae. Disulfides 8-17 lysozyme Homo sapiens 58-66 3288200-2 1988 Our results have revealed that the formation of the disulfide bond Cys6/Cys128 in human lysozyme is a prerequisite for correct folding in vivo in yeast. Disulfides 52-61 lysozyme Homo sapiens 88-96 3288200-5 1988 These are the first findings that the individual disulfide bonds of human lysozyme have different functions in folding and secretion in vivo. Disulfides 49-58 lysozyme Homo sapiens 74-82 6276374-3 1982 Thus, to address this problem, disulfide bonds of ribonuclease-A and lysozyme were reductively cleaved under denaturing conditions, and the resulting 7-8 sulfhydryl groups were treated with a new sulfhydryl group reagent containing selenium, 6,6"-diselenobis(3-nitrobenzoic acid), to give proteins containing covalently attached selenium in the form of selenenyl sulfides. Disulfides 31-40 lysozyme Homo sapiens 69-77 7440057-0 1980 Preparation of a two-disulfide bonded enzymically active derivative from hen egg lysozyme. Disulfides 21-30 lysozyme Homo sapiens 81-89 7440057-1 1980 A method has been developed for preparation of an enzymically active two-disulfide bonded derivative from hen egg lysozyme. Disulfides 73-82 lysozyme Homo sapiens 114-122 7440057-7 1980 Thus, the species containing two presumably native disulfide bonds and four free sulfhydryl groups at Cys 6, Cys 76, Cys 94 and Cys 127 appears to be only the intermediate accumulating during reduction of lysozyme with dithiothreitol. Disulfides 51-60 lysozyme Homo sapiens 205-213 1254590-8 1976 Accessibility to tryptic hydrolysis and susceptibility of the disulfide bonds to reduction were increased in the derivative relative to lysozyme. Disulfides 62-71 lysozyme Homo sapiens 136-144 34197967-4 2021 An antibacterial enzyme, lysozyme, was then conjugated on the surface of the nanocomposite by a cleavable disulfide linker, resulting in a redox-sensitive nanoplatform. Disulfides 106-115 lysozyme Homo sapiens 25-33 7150571-2 1982 After initiation of disulfide bond formation associated with the folding process of reduced human lysozyme, molecules have been trapped in a stable form with iodoacetic acid (preserving disulfide bonds) at various times of reoxidation. Disulfides 20-29 lysozyme Homo sapiens 98-106 7150571-2 1982 After initiation of disulfide bond formation associated with the folding process of reduced human lysozyme, molecules have been trapped in a stable form with iodoacetic acid (preserving disulfide bonds) at various times of reoxidation. Disulfides 186-195 lysozyme Homo sapiens 98-106 241414-2 1975 Reduction of lysozyme by diborane, followed by air oxidation of the reduced disulfides and chromatography on CM-cellulose, yielded a homogeneous derivative. Disulfides 76-86 lysozyme Homo sapiens 13-21 241414-4 1975 Correct re-forming of the disulfide bonds was demonstrated by peptide mapping of the tryptic hydrolysates of the derivative and lysozyme without breaking the disulfide bonds, followed by identification of the disulfide-containing peptides. Disulfides 26-35 lysozyme Homo sapiens 128-136 241414-6 1975 Preparations of the two-disulfide fragment from lysozyme and derivative had equal inhibitory activities (26 or 32%) of the reaction of lysozyme with two homologous antisera. Disulfides 24-33 lysozyme Homo sapiens 48-56 241414-6 1975 Preparations of the two-disulfide fragment from lysozyme and derivative had equal inhibitory activities (26 or 32%) of the reaction of lysozyme with two homologous antisera. Disulfides 24-33 lysozyme Homo sapiens 135-143 1164516-8 1975 However, their disulfide bonds were slightly more accessible to reduction than lysozyme, with the increase being somewhat higher in derivatives I, II and III. Disulfides 15-24 lysozyme Homo sapiens 79-87 14189889-0 1964 INTERACTION OF PHOSPHOROTHIOATE WITH THE DISULFIDE BONDS OF RIBONUCLEASE AND LYSOZYME. Disulfides 41-50 lysozyme Homo sapiens 77-85 33136395-11 2021 All four disulfide bonds of lysozyme were determined. Disulfides 9-18 lysozyme Homo sapiens 28-36 34002274-3 2021 An MIP film for lysozyme was prepared by the copolymerization of {[2-(2-methacrylamido)ethyldithio]ethylcarbamoyl}methoxy acetic acid, a functional monomer possessing a modifiable disulfide bond, with acrylamide and N,N"-methylenebisacrylamide in the presence of lysozyme. Disulfides 180-189 lysozyme Homo sapiens 16-24 34002274-4 2021 After the removal of lysozyme, the disulfide bonds were cleaved by treatment with a reductant. Disulfides 35-44 lysozyme Homo sapiens 21-29 32939274-4 2020 A careful analysis of the chemical environment of disulfide bonds in the structures of elastase, lysozyme, acetylcholinesterase and other proteins suggests that S-S bonds which engage in a close contact with a carbonyl O atom along the extension of the S-S bond vector are more susceptible to reduction than the others. Disulfides 50-59 lysozyme Homo sapiens 97-105 32971812-4 2020 The data from the molten globule-like structures of ribonuclease, lysozyme, bovine serum albumin and chymotrypsinogen identified new speeding agents, i.e., hydrophobic/electrostatic interactions and productive complex formations involving the protein and thiol reagent, which were able to confer exceptional reactivity to structural cysteines which were only intended to form disulfides. Disulfides 376-386 lysozyme Homo sapiens 66-74 31458105-8 2018 We further show that GdmCl denatures lysozyme with the disulfide bonds intact in the protein, whereas urea denatures the protein only when the disulfide bonds are broken using reducing agents. Disulfides 55-64 lysozyme Homo sapiens 37-45 30913878-0 2019 Role of Disulfide Bonds and Topological Frustration in the Kinetic Partitioning of Lysozyme Folding Pathways. Disulfides 8-17 lysozyme Homo sapiens 83-91 30913878-2 2019 Lysozyme has four disulfide bonds and is widely studied for its antibacterial properties. Disulfides 18-27 lysozyme Homo sapiens 0-8 30913878-5 2019 Using a coarse-grained protein model and simulations, we show that two out of the four disulfide bonds, which are present in the alpha-domain of lysozyme, are responsible for the slow folding pathway. Disulfides 87-96 lysozyme Homo sapiens 145-153 30913878-14 2019 These results show that lysozyme also serves as a very good model system to probe the role of disulfide bonds and topological frustration in protein folding. Disulfides 94-103 lysozyme Homo sapiens 24-32 30375487-2 2018 Here we show that egg lysozyme displays a clever strategy to prevent this deleterious aggregation during the nascent phase when disulfides are still absent. Disulfides 128-138 lysozyme Homo sapiens 22-30 31877449-2 2020 While secondary structural propensity of both proteins is larger in glycerol, results for tertiary structure and translational diffusion coefficient with increasing glycerol provide two contrasting depictions - lysozyme becomes increasingly compact, plausibly due to disulfide bridge constraints, but cytochrome c expands and loses the tertiary structure. Disulfides 267-276 lysozyme Homo sapiens 211-219 30830762-5 2019 Mixtures of holo- and apo-myoglobin (Mb) and disulfide isomers of lysozyme (Lyz) were characterized in a conformer-specific fashion using this strategy, followed by conformation interrogation for the sequentially eluted 2H-labeled species in real-time using top-down MS. Disulfides 45-54 lysozyme Homo sapiens 66-74 30830762-6 2019 Under mildly denaturing conditions that minimize the charge difference, disulfide isomers of Lyz were differentially labeled with 2H during separation based on their disulfide-dependent sizes. Disulfides 72-81 lysozyme Homo sapiens 93-96 30830762-6 2019 Under mildly denaturing conditions that minimize the charge difference, disulfide isomers of Lyz were differentially labeled with 2H during separation based on their disulfide-dependent sizes. Disulfides 166-175 lysozyme Homo sapiens 93-96 30009290-3 2018 In particular, we demonstrate that the native tertiary structure of lysozyme is preserved if, and only if, its four intramolecular disulfide bridges are intact. Disulfides 131-140 lysozyme Homo sapiens 68-76 27966089-6 2017 Raman shifts and the alteration of spectral features observed in the ClO2-treated lysozyme samples are associated with loss of the alpha-helix secondary structure, tertiary structure, and disulfide bond. Disulfides 188-197 lysozyme Homo sapiens 82-90 27086995-1 2016 Disulfide bond shuffling in the presence of the reducing agents dithiothreitol (DTT) or beta-mercaptoethanol (BME) strongly affects the surface properties of lysozyme solutions. Disulfides 0-9 lysozyme Homo sapiens 158-166 25359082-6 2014 MALDI-TOF/TOF revealed that papain degraded LYS, giving rise to three IgE-binding fragments: LYS (22-129), LYS (34-96) and LYS (62-128) that likely remained linked through the disulfide bonds present in the LYS molecule. Disulfides 176-185 lysozyme Homo sapiens 44-47 25363360-7 2014 The inner layer of LSZ is assumed to bind firmly to silver via disulfide bridges, which makes it irreversibly adsorbed with respect to dilution. Disulfides 63-72 lysozyme Homo sapiens 19-22