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Article

Phi-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy.

Proceedings of the National Academy of Sciences of the United States of America - 2 Oct 2007

Neudecker Philipp, Zarrine-Afsar Arash, Davidson Alan R, Kay Lewis E

Abstract excerpt

Experimental studies of protein folding frequently are consistent with two-state folding kinetics. However, recent NMR relaxation dispersion studies of several fast-folding mutants of the Fyn Src homology 3 (SH3) domain have established that folding proceeds through a low-populated on-pathway intermediate, which could not be detected with stopped-flow experiments. The dispersion experiments provide precise...

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Identifiers

PMID: 17898173
DOI: 10.1073/pnas.0705097104
PMCID: PMC2000424

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