CEESY:  Characterizing the Conformation of Unobservable Protein States

Protein conformations that are only marginally populated often play important roles as intermediate states in many processes such as ligand binding, enzyme catalysis, allostery, and protein folding. An NMR method is presented that can give valuable information about the structure of these “excited s...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2006-03, Vol.128 (12), p.3856-3857
Main Authors: van Ingen, Hugo, Vuister, Geerten W, Wijmenga, Sybren, Tessari, Marco
Format: Article
Language:English
Subjects:
Nuclear Magnetic Resonance, Biomolecular - methods
Protein Conformation
Proteins - chemistry
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Summary:Protein conformations that are only marginally populated often play important roles as intermediate states in many processes such as ligand binding, enzyme catalysis, allostery, and protein folding. An NMR method is presented that can give valuable information about the structure of these “excited states” by measuring the relative position of exchanging excited- and ground-state resonances using a single 2D spectrum. This new approach can be applied to any nucleus, which will facilitate a complete structural characterization of these states.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja0568749