The origin of pH-dependent changes in m-values for the denaturant-induced unfolding of proteins.

doi:10.1006/jmbi.2001.4726

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Article

The origin of pH-dependent changes in m-values for the denaturant-induced unfolding of proteins.

Journal of molecular biology - 22 Jun 2001

Whitten S T, Wooll J O, Razeghifard R, García-Moreno E B, Hilser V J

Abstract excerpt

Denaturant-induced unfolding is one of the most prevalent means of evaluating the structural stability of proteins and of determining the energetic consequences of mutations or changes in solution conditions. In spite of the widespread use of this approach, controversies and inconsistencies still persist with regard to the interpretation of the results of such studies. For example, most proteins show either a...

Topics

Acids
Computer Simulation
Enzyme Stability
Hydrogen-Ion Concentration
Micrococcal Nuclease
Mutation
Protein Denaturation
Protein Folding
Protons
Thermodynamics
Urea

Source

Open in PubMed

Identifiers

PMID: 11399086
DOI: 10.1006/jmbi.2001.4726

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