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PMID: 15808225 Published · ppublish English Journal Article

Elucidation of the protein folding landscape by NMR.

Methods in enzymology ·Vol. 394 ·2005-00-00 ·Pages 299-321

Dyson HJ, Wright PE

Abstract

NMR is one of the few experimental methods that can provide detailed insights into the structure and dynamics of unfolded and partly folded states of proteins. Mapping the protein folding landscape is of central importance to understanding the mechanism of protein folding. In addition, it is now recognized that many proteins are intrinsically unstructured in their functional states, while partly folded states of several cellular proteins have been implicated in amyloid disease. NMR is uniquely suited to characterize the structures present in the conformational ensemble and probe the dynamics of the polypeptide chain in unfolded and partially folded protein states.

MeSH Terms
Magnetic Resonance Spectroscopy/methods Protein Folding Protein Structure, Tertiary
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Dyson H Jane
Department of Molecular Biology and Skaggs Institute for Chemical Research, Scripps Research Institute, La Jolla, California 92037, USA.
Wright Peter E
Article Info
Journal
Methods in enzymology
Abbr.
Methods Enzymol
ISSN
0076-6879
Published
2005-00-00
Pages
299-321
Language
English
Region
United States
NLM ID
0212271
Subset
IM
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