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PubMed · 15609984

Monitoring protein folding at atomic resolution.

Thallapuranam Krishnaswamy S Kumar·Chin Yu
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Abstract

Elucidation of the mechanisms by which proteins fold from disordered conformations to their unique native conformations is one of the most challenging tasks facing structural biologists. Understanding the mechanism(s) of protein folding involves the characterization of all structural species that occur in the protein-folding reaction. Nuclear magnetic resonance (NMR) spectroscopy is a powerful and versatile technique that provides an avenue to investigate the structures of the various conformational states at the residue level along the protein-folding reaction coordinate. In this Account, we provide a comprehensive review of the recent progress on the applications of NMR to monitor equilibrium and kinetic conformational states of the protein-folding reaction.

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ApoproteinsFibroblast Growth Factor 1HydrogenKineticsMyoglobinNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein DenaturationProtein FoldingProteinsJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.Review

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Thallapuranam Krishnaswamy S Kumar, Chin Yu. 2004. Monitoring protein folding at atomic resolution.. https://doi.org/10.1021/ar020156z

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