Monitoring protein folding at atomic resolution

by Kumar, T. K. S.; Yu, C.

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.

Journal
Accounts of Chemical Research
Volume
37
Issue
12
Year
2004
Start Page
929-936
URL
https://dx.doi.org/10.1021/ar020156z
ISBN/ISSN
1520-4898; 0001-4842
DOI
10.1021/ar020156z