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Collapse of the hydration shell of a protein prior to thermal unfolding
Author(s) -
Koizumi Masaharu,
Hirai Harutaka,
Onai Teruaki,
Inoue Katsuaki,
Hirai Mitsuhiro
Publication year - 2007
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s0021889807003354
Subject(s) - lysozyme , radius of gyration , shell (structure) , chemistry , solvation shell , crystallography , small angle x ray scattering , scattering , thermodynamics , chemical physics , materials science , polymer , physics , molecule , organic chemistry , solvation , optics , biochemistry , composite material
Based on high statistical quality wide‐angle X‐ray scattering data for the unfolding–refolding process of hen egg‐white lysozyme (HEWL), we have analysed the change of the hydration shell as a function temperature using the program CRYSOL . The present results suggest that the decrease of the hydration‐shell density starts from a lower temperature than the transition temperature of the collapse of the tertiary structure of HEWL. Although the use of CRYSOL for scattering data for proteins before the transition has an apparent limitation, the collapse of the hydration shell prior to the unfolding of HEWL agrees with a slight tendency of the radius of gyration to decrease during the thermal unfolding process.