Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfolding.

[1]  R. S. Spolar,et al.  Contribution to the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface area. , 1991, Biochemistry.

[2]  B. Wunderlich,et al.  Heat capacities of solid poly(amino acids). I. Polyglycine, poly(L‐alanine), and poly(L‐valine) , 1991 .

[3]  K. P. Murphy,et al.  Group additivity thermodynamics for dissolution of solid cyclic dipeptides into water , 1990 .

[4]  P. Privalov,et al.  Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: protein unfolding effects. , 1990, Journal of molecular biology.

[5]  P. Privalov,et al.  Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: hydration effect. , 1990, Journal of molecular biology.

[6]  R. S. Spolar,et al.  Hydrophobic effect in protein folding and other noncovalent processes involving proteins. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[7]  P. Privalov,et al.  Heat capacity of alcohols in aqueous solutions in the temperature range from 5 to 125°C , 1989 .

[8]  P. Privalov,et al.  Heat capacity and conformation of proteins in the denatured state. , 1989, Journal of molecular biology.

[9]  O. Ptitsyn Protein folding: Hypotheses and experiments , 1987 .

[10]  S. Gill,et al.  Heat of solution of methane in water from 0 to 50.degree.C , 1986 .

[11]  J M Sturtevant,et al.  Thermodynamics of the denaturation of lysozyme in alcohol--water mixtures. , 1979, Biochemistry.

[12]  J M Sturtevant,et al.  Heat capacity and entropy changes in processes involving proteins. , 1977, Proceedings of the National Academy of Sciences of the United States of America.

[13]  S. Gill,et al.  An equation of state describing hydrophobic interactions. , 1976, Proceedings of the National Academy of Sciences of the United States of America.

[14]  A. Haly,et al.  Calorimetry of rat tail tendon collagen before and after denaturation: the heat of fusion of its absorbed water , 1971, Biopolymers.

[15]  K. Kuwajima,et al.  The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structure , 1989, Proteins.

[16]  Privalov Pl,et al.  Thermodynamic Problems of Protein Structure , 1989 .

[17]  P. Privalov,et al.  Stability of protein structure and hydrophobic interaction. , 1988, Advances in protein chemistry.

[18]  S. Gill,et al.  Heats of solution of ethane and propane in water from 0 to 50.degree.C , 1987 .

[19]  P. Privalov Stability of proteins: small globular proteins. , 1979, Advances in protein chemistry.