Properties of hydration shells of protein molecules at their pressure- and temperature-induced native-denatured transition.
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 sigma are investigated with the help of the equation of state of water in an open system. The local values of sigma rather close to each other (sigma(D) approximately 0.3 C m(-2)) are found for six different experimental lines of the N-D transition found in the literature. The values sigma(D) correspond to the crossings of the total pressure (P(t)+Pi) vs sigma isotherms at different T(t) (Pi-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.
Danielewicz-Ferchmin
Irena
I
Faculty of Physics, A. Mickiewicz University Umultowska 85, 61-614 Poznań, Poland.
Banachowicz
Ewa M
EM
Ferchmin
A Ryszard
AR
D011312:Pressure; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry*; D012997:Solvents / Q000737:chemistry; D013499:Surface Properties; D013696:Temperature; D013816:Thermodynamics; D014867:Water / Q000737:chemistry*
D011506:Proteins; D012997:Solvents; D014867:Water