Journal article
Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding
Protein science, Vol.4(10), pp.2138-2148
10/1995
DOI: 10.1002/pro.5560041020
PMCID: PMC2142997
PMID: 8535251
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.
Details
- Title: Subtitle
- Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding
- Creators
- J K Myers - Texas A&M UniversityC N Pace - Texas A&M UniversityJ M Scholtz - Texas A&M University
- Resource Type
- Journal article
- Publication Details
- Protein science, Vol.4(10), pp.2138-2148
- DOI
- 10.1002/pro.5560041020
- PMID
- 8535251
- PMCID
- PMC2142997
- ISSN
- 0961-8368
- eISSN
- 1469-896X
- Grant note
- T32 GM08523 / NIGMS NIH HHS R01 GM37039 / NIGMS NIH HHS R29 GM52483 / NIGMS NIH HHS
- Language
- English
- Date published
- 10/1995
- Academic Unit
- Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
- Record Identifier
- 9984293079702771
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