title: Downhill protein folding: evolution meets physics.
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.
authors.affiliation: Department of Chemistry, University of Illinois, Urbana, IL 61801, USA. gruebele@scs.uiuc.edu
authors.forename: Martin
authors.initials: M
authors.lastname: Gruebele
mesh_terms: D000818:Animals; D004777:Environment; D019143:Evolution, Molecular; D005815:Genetic Code; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D013816:Thermodynamics
chemical_list: D011506:Proteins