PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23109228-2 2013 The active site of hen egg-white lysozyme (HEWL) is believed to consist of six subsites, A-F that can accommodate six sugar residues. Sugars 118-123 lysozyme Homo sapiens 33-41 20059115-0 2009 Low-frequency vibrational properties of lysozyme in sugar aqueous solutions: a Raman scattering and molecular dynamics simulation study. Sugars 52-57 lysozyme Homo sapiens 40-48 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. Sugars 141-147 lysozyme Homo sapiens 109-117 22909409-1 2012 The effect of the sugars sucrose, glucose, and trehalose on the structural and colloidal stability of lysozyme has been investigated using differential scanning calorimetry and quasi-elastic light scattering, respectively. Sugars 18-24 lysozyme Homo sapiens 102-110 20059115-1 2009 The low-frequency (omega<400 cm(-1)) vibrational properties of lysozyme in aqueous solutions of three well-known protecting sugars, namely, trehalose, maltose, and sucrose, have been investigated by means of complementary Raman scattering experiments and molecular dynamics simulations. Sugars 127-133 lysozyme Homo sapiens 66-74 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. Sugars 27-33 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. Sugars 27-33 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. Sugars 27-33 lysozyme Homo sapiens 237-245 2302221-1 1990 The effects of sugars and similar additives on the catalytic activity of lysozyme have been attributed (Laretta-Garde et al., Biochim. Sugars 15-21 lysozyme Homo sapiens 73-81 12429473-4 2002 It has been shown that by co-dissolving various sugars and polyhydric alcohols with lysozyme in the first aqueous buffer, interface-induced lysozyme aggregation and inactivation can be minimized in the first emulsification step [J. Pharm. Sugars 48-54 lysozyme Homo sapiens 84-92 12429473-4 2002 It has been shown that by co-dissolving various sugars and polyhydric alcohols with lysozyme in the first aqueous buffer, interface-induced lysozyme aggregation and inactivation can be minimized in the first emulsification step [J. Pharm. Sugars 48-54 lysozyme Homo sapiens 140-148 11948532-6 2002 The presence of both sugars led to increased T(1) values of the lysozyme but increasing hydration gradually reduced T(1) values. Sugars 21-27 lysozyme Homo sapiens 64-72 11948532-9 2002 Trehalose and lactose decreased relaxation rates in the lysozyme-sugar systems while hydration increased relaxation rates that were correlated with changes in aggregation and activity of the protein. Sugars 65-70 lysozyme Homo sapiens 56-64 8885835-2 1996 Under the conditions comprising 2.0 x 10(-3) M labeling reagent and 1.0 x 10(-5) M human lysozyme at pH 5.4, 37 degrees C, the reaction time required to reduce the lytic activity against Micrococcus luteus cells to 50% of its initial activity was lengthened by 3.7 times through the substitution of the nonreducing end sugar residue, GlcNAc to Gal. Sugars 319-324 lysozyme Homo sapiens 89-97 11948532-1 2002 The molecular mobility of protein in lyophilized lysozyme-sugar systems stored at different relative humidities was studied using solid-state NMR. Sugars 58-63 lysozyme Homo sapiens 49-57 7142111-3 1982 It has been reported that binding subsite D in human lysozyme has negative free energy on substrate binding, whereas subsite D in hen lysozyme has unfavorable positive free energy due to the distortion of a sugar residue. Sugars 207-212 lysozyme Homo sapiens 53-61 7142111-3 1982 It has been reported that binding subsite D in human lysozyme has negative free energy on substrate binding, whereas subsite D in hen lysozyme has unfavorable positive free energy due to the distortion of a sugar residue. Sugars 207-212 lysozyme Homo sapiens 134-142 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. Sugars 107-112 lysozyme Homo sapiens 34-42 497177-5 1979 The magnitude of the stabilizing effect (delta Tm) depended on both the nature of the protein and the nature of the sugar or polyol, ranging from 18.5 degrees C for lysozyme at pH 3 in the presence of 50% (w/w) sorbitol to 0 degrees C for conalbumin at pH 7 in 50% glycerol solution. Sugars 116-121 lysozyme Homo sapiens 165-173 29488193-6 2018 Our results elucidated several relevant formulation attributes (density, total solid content, protein:sugars ratio) required to achieve a stable lysozyme powder with desirable characteristics for pulmonary delivery. Sugars 102-108 lysozyme Homo sapiens 145-153