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Conformational Dynamics and Ensembles in Protein Folding

AutorMuñoz van den Eynde, Víctor
Palabras claveProtein folding
Polypeptide motions
Downhill folding
Folding barriers
Noncovalent interactions
Fecha de publicación9-feb-2007
EditorAnnual Reviews
CitaciónAnnual Review of Biophysics and Biomolecular Structure 36: 395-412 (2007)
ResumenRecent experimental developments are changing the ways we interpret experimental data in protein folding, leading to a closer connection with theory and an improved understanding of some long-standing questions in the field. We now have a basic roadmap of the types of polypeptide motions and timescales that are relevant to the various folding stages. The folding barriers estimated with a variety of independent methods are consistently small, indicating that several fast-folding proteins are near or within the downhill folding regime. Finally, the structural and statistical analysis of global downhill folding is promising to open a new avenue of research in which folding mechanisms and the networks of noncovalent interactions that stabilize native structures are directly resolved in equilibrium experiments of nonmutated proteins.
Descripción18 pages.-- PMID: 17291180 [PubMed].-- Printed version published on Jun 2007.
Versión del editorhttp://dx.doi.org/10.1146/annurev.biophys.36.040306.132608
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