Chemical denaturation: Potential impact of undetected intermediates in the free energy of unfolding and m-values obtained from a two-state assumption

Biophysical Journal

Volumn 75, Issue 1, 1998, Pages 484-492

  Soulages, Jose L ^a  

^a University of Arizona   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CHEMICAL REACTION KINETICS; EQUILIBRIUM CONSTANT; PATIENT MONITORING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; SIMULATION;

EID: 0031808804     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77537-X     Document Type: Article

References (19)

1. Barrick, D., and R. L. Baldwin. 1993. Three-state analysis of sperm whale apomyoglobin folding. Biochemistry. 32:3790-3796.
2. Brandts, J. F. 1969. Conformational transitions of proteins in water and aqueous mixtures. In Structure and Stability of Biological Macromolecules. S. N. Timasheff and Fasman, G. D., editors. Marcel Dekker, New York. 213-290.
3. Carra, J. H., E. A. Anderson, and P. L. Privalov. 1994. Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants. Biochemistry. 33:10842-10850.
4. Carra, J. H., and P. L. Privalov. 1995. Energetics of denaturation and m-values of staphylococcal nuclease mutants. Biochemistry. 34: 2034-2041.
5. Fink, A. L. 1995. Molten globules. Methods Mol. Biol. 40:343-360.
6. Greene, R. F. J., and C. N. Pace. 1974. Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, alpha-chymotrysin and beta-lactaglobulin. J. Biol. Chem. 249:5388-5393.
7. Kim, P. S., and R. L. Baldwin. 1990. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:631-660.
8. Kuwajima, K., K. Nitta, M. Yoneyama, and S. Sugai. 1976. Three-state denaturation of α-lactalbumin by guanidine hydrochloride. J. Mol. Biol. 106:359-373.
9. Matthews, B. W. 1995. Studies on protein stability with T4 lysozyme. Adv. Prot. Chem. 46:249-278
10. Pace, N. C. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:266-280.
11. Privalov, P. L. 1979. Stability of proteins: small globular proteins. Adv. Prot. Chem. 33:167-197.
12. Ptitsyn, O. B. 1992. The molten globule state. In Protein Folding. T. E. Creighton, editor. Freeman, New York. 243-300.
13. Ptitsyn, O. B. 1995. Molten globule and protein folding. Adv. Protein Chem. 47:83-229.
14. Santoro, M. M., and D. W. Bolen. 1988. Unfolding free energy changes determined by the linear extrapolation method. I. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry. 27:8063-8068.
15. Santoro, M. M., and D. W. Bolen. 1992. A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range. Biochemistry. 31:4901-4907.
16. Schellman, J. 1978. Solvent denaturation. Biopolymers. 17:1305-1322.
17. Shortle, D. 1989. Probing the determinants of protein folding and stability with amino acid substitutions. J. Biol. Chem. 264:5315-5318.
18. Shortle, D. 1995. Staphylococcal nuclease: a showcase of m-value effects. Adv. Prot. Chem. 46:217-278.
19. Yao, M., and D. W. Bolen. 1995. How valid are the denaturant-induced unfolding free-energy measurements? level of conformance to common assumptions over an extended range of ribonuclease A stability. Biochemistry. 34:3771-3781.