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PMID: 8535251 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

Protein science : a publication of the Protein Society ·Vol. 4 ·No. 10 ·1995-10-00 ·Pages 2138-48

Myers JK, Pace CN, Scholtz JM

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.

MeSH Terms
Animals Calorimetry Enzymes/chemistry Guanidine Guanidines Hot Temperature Humans Kinetics Mathematics Muramidase/chemistry Protein Denaturation Protein Folding Proteins/chemistry Regression Analysis Ribonuclease T1/chemistry Ribonucleases/chemistry Thermodynamics
Chemicals
Enzymes Guanidines Proteins Ribonucleases Ribonuclease T1 Muramidase Guanidine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Myers J K
Department of Biochemistry and Biophysics, Texas A&M University, College Station 77843, USA.
Pace C N
Scholtz J M
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Article Info
Journal
Protein science : a publication of the Protein Society
Abbr.
Protein Sci
ISSN
0961-8368
DOI
10.1002/pro.5560041020
Published
1995-10-00
Pages
2138-48
Language
English
Region
United States
NLM ID
9211750
PMCID
PMC2142997
Subset
IM
Grants
NIGMS NIH HHS · R01 GM37039 · United States
NIGMS NIH HHS · R29 GM52483 · United States
NIGMS NIH HHS · T32 GM08523 · United States
Corrections
ErratumIn
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External Links
PubMed source DOI: 10.1002/pro.5560041020 PMC Full Text View journal details
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