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Review
. 2007:36:395-412.
doi: 10.1146/annurev.biophys.36.040306.132608.

Conformational dynamics and ensembles in protein folding

Affiliations
Review

Conformational dynamics and ensembles in protein folding

Victor Muñoz. Annu Rev Biophys Biomol Struct. 2007.

Abstract

Recent 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.

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