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Properties of Hydration Shells of Protein Molecules at their Pressure‐ and Temperature‐Induced Native‐Denatured Transition
Author(s) -
DanielewiczFerchmin Irena,
Banachowicz Ewa M.,
Ferchmin A. Ryszard
Publication year - 2006
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.200600289
Subject(s) - chemistry , molecule , electrostriction , crystallography , thermodynamics , materials science , organic chemistry , physics , piezoelectricity , composite material
Properties of water at the surface of biomolecules are important for their conformational stability. The behaviour of hydrating water at protein transition (t) pressures P t and temperatures T t , with the points ( P t ,T t ) lying in the Native–Denatured (N‐D) transition line, is studied. Hydration shells at the hydrophilic regions of protein molecules with surface charge density σ are investigated with the help of the equation of state of water in an open system. The local values of σ rather close to each other ( σ D ≈0.3 C m −2 ) are found for six different experimental lines of the N‐D transition found in the literature. The values σ D correspond to the crossings of the total pressure ( P t + Π ) vs σ isotherms at different T t ( Π −electrostriction pressure). The pressures P t and temperatures T t appear to be related with some selected sites at the surfaces of the protein molecules.