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Protein Sci. 1995 Oct;4(10):2138-48.

Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding.

Author information

1
Department of Biochemistry and Biophysics, Texas A&M University, College Station 77843, USA.

Erratum in

  • Protein Sci 1996 May;5(5):981.

Abstract

Denaturant m values, the dependence of the free energy of unfolding on denaturant concentration, have been collected for a large set of proteins. The m value correlates very strongly with the amount of protein surface exposed to solvent upon unfolding, with linear correlation coefficients of R = 0.84 for urea and R = 0.87 for guanidine hydrochloride. These correlations improve to R = 0.90 when the effect of disulfide bonds on the accessible area of the unfolded protein is included. A similar dependence on accessible surface area has been found previously for the heat capacity change (delta Cp), which is confirmed here for our set of proteins. Denaturant m values and heat capacity changes also correlate well with each other. For proteins that undergo a simple two-state unfolding mechanism, the amount of surface exposed to solvent upon unfolding is a main structural determinant for both m values and delta Cp.

PMID:
8535251
PMCID:
PMC2142997
DOI:
10.1002/pro.5560041020
[Indexed for MEDLINE]
Free PMC Article

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