title: Elucidation of the protein folding landscape by NMR.
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.
authors.affiliation: Department of Molecular Biology and Skaggs Institute for Chemical Research, Scripps Research Institute, La Jolla, California 92037, USA.
authors.forename: H Jane
authors.initials: HJ
authors.lastname: Dyson
authors.forename: Peter E
authors.initials: PE
authors.lastname: Wright
mesh_terms: D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D017510:Protein Folding; D017434:Protein Structure, Tertiary