Conformational dynamics and ensembles in protein folding.
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.
Muñoz
Victor
V
Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, USA. vmunoz@umd.edu
D000818:Animals; D003198:Computer Simulation; D006801:Humans; D007700:Kinetics; D008962:Models, Theoretical; D008968:Molecular Conformation; D009038:Motion; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D013053:Spectrophotometry; D013816:Thermodynamics
D011506:Proteins