Desolvation is a likely origin of robust enthalpic barriers to protein folding.

doi:10.1016/j.jmb.2005.03.084

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Article

Desolvation is a likely origin of robust enthalpic barriers to protein folding.

Journal of molecular biology - 17 Jun 2005

Liu Zhirong, Chan Hue Sun

Abstract excerpt

Experimental data from global analyses of temperature (T) and denaturant dependence of the folding rates of small proteins led to an intrinsic enthalpic folding barrier hypothesis: to a good approximation, the T-dependence of folding rate under constant native stability conditions is Arrhenius. Furthermore, for a given protein, the slope of isostability folding rate versus 1/T is essentially independent of native...

Topics

Animals
Kinetics
Models, Chemical
Mutation
Protein Folding
Proteins
Solvents
Thermodynamics

Source

Open in PubMed

Identifiers

PMID: 15893325
DOI: 10.1016/j.jmb.2005.03.084

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