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.