Thermodynamic properties of globular proteins and the principle of stabilization of their native structure.
A semi-empirical method has been used to estimate the thermodynamic parameters of hydration of buried surface areas of ribonuclease S, lysozyme and myoglobin from the model of complete unfolding according to Ooi et al. ((1987) Proc. Natl. Acad. Sci. USA 84, 3086-3090). The buried surface area of proteins is considered as the difference between the accessible surface area of native protein and the completely extended polypeptide chain according to Lee and Richards ((1971) J. Mol. Biol. 55, 379-400). The contributions of nonpolar and polar protein groups to the general value of Gibbs energy, enthalpy, entropy and heat capacity of hydration have been determined. The obtained results on the thermodynamic behavior of proteins in the process of complete unfolding are in good agreement with the results of microcalorimetric studies of thermal denaturation.
Khechinashvili
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Institute of Biological Physics, Academy of Sciences, U.S.S.R., Moscow Region.
D000818:Animals; D002151:Calorimetry; D066298:In Vitro Techniques; D009113:Muramidase; D009211:Myoglobin; D011487:Protein Conformation; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry*; D012259:Ribonuclease, Pancreatic; D012260:Ribonucleases; D013696:Temperature; D013816:Thermodynamics; D014867:Water
D009211:Myoglobin; D011506:Proteins; D014867:Water; D012260:Ribonucleases; D012259:Ribonuclease, Pancreatic; C022542:ribonuclease S; D009113:Muramidase