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Downhill protein folding: evolution meets physics
Authors:Gruebele Martin
Affiliation:Department of Chemistry, University of Illinois, Urbana, IL 61801, USA. gruebele@scs.uiuc.edu
Abstract:Proteins can be redesigned to fold downhill on a free energy surface characterized by only a few coordinates, confirming a principal prediction of the 'energy-landscape' model. Nonetheless, natural proteins have small but significant barriers. Spectroscopy and kinetics reveal potential biological causes for activation barriers during protein folding: evolution against protein aggregation and for protein function.
Keywords:Protein function  Temperature jump  Hydrophobicity  Activation barrier  Fonction de la protéine  Saut de température  Hydrophobicité  Barrière d'activation
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