2021
DOI: 10.1016/j.bbrep.2021.101184
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The role of water in the reversibility of thermal denaturation of lysozyme in solid and liquid states

Abstract: Although unfolding of protein in the liquid state is relatively well studied, its mechanisms in the solid state, are much less understood. 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. Analysis of the endothermic thermal transition obtained by DSC scans showed three distinct… Show more

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Cited by 12 publications
(16 citation statements)
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References 34 publications
(42 reference statements)
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“…These examples demonstrate that the model provides a reasonable fit to the experimental data; moreover, the obtained parameters such as ellipsoid radii and volume fractions are physically meaningful. For example, the ellipsoid radii at temperatures below denaturation are close to the ellipsoid parameters obtained in the liquid . This suggests that the protein molecules in the solid state in the presence of sucrose retain shapes close to their native shape (observed in aqueous solutions).…”
Section: Resultssupporting
confidence: 70%
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“…These examples demonstrate that the model provides a reasonable fit to the experimental data; moreover, the obtained parameters such as ellipsoid radii and volume fractions are physically meaningful. For example, the ellipsoid radii at temperatures below denaturation are close to the ellipsoid parameters obtained in the liquid . This suggests that the protein molecules in the solid state in the presence of sucrose retain shapes close to their native shape (observed in aqueous solutions).…”
Section: Resultssupporting
confidence: 70%
“…Figure shows the denaturation peak of lysozyme at different sucrose concentrations both for samples with residual moisture as well as dried samples. The T d in freeze-dried mixtures is higher than in lysozyme–water mixtures in the solid or liquid state . The calorimetric enthalpy (Table ) has similar values to the enthalpy in aqueous solution .…”
Section: Resultsmentioning
confidence: 78%
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“…From these crystals, no X-ray diffractions were observed under cryogenic conditions, indicating their loss of diffraction ability throughout the soaking operation. Because the crystal shapes were maintained during a week of soaking, the acid/base denaturation of proteins in the cross-linked crystals, resulting in the amorphous solid state, could be limited to their partial unfolding ( Phan-Xuan et al, 2021 ). Indeed, pH is known to influence the stability of proteins by altering the net charge on the proteins, and many proteins denature at extremes of pH because of the presence of destabilizing intramolecular electrostatic interactions ( Fink et al, 1994 ; Khurana et al, 1995 ; Dwyer et al, 2000 ).…”
Section: Resultsmentioning
confidence: 99%