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- W2028731267 abstract "Abstract In this study variations with respect to temperature of entropy increment Δ S , arising in the dissolution of proteins in water, have been investigated by the methods of statistical thermodynamics. In this formalism, effective electric field E and total dipole moment M are taken as thermodynamical variables. The partition function given by Bakk et al. [Physica A 304 (2002) 355–361] has been used in a modified form while obtaining the free energy. In the constructed phenomenological theory, experimental data are taken from the study of Privalov [J. Chem. Thermodyn. 29 (1997) 447–474; J. Mol. Biol. 213 (1990) 385; T.E. Creighton, Protein Folding, W.H. Freeman and Company, New York, 1995, pp. 83–151] and relevant parameters have been found by fitting to experimental curves. The variations of entropy increments Δ S have been investigated in the temperature range 265– 350 K ." @default.
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- W2028731267 date "2006-02-01" @default.
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- W2028731267 title "Investigation of hydration effect of the proteins by phenomenological thermostatistical methods" @default.
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- W2028731267 doi "https://doi.org/10.1016/j.physa.2005.07.004" @default.
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