title: Fast protein folding on downhill energy landscape.
abstract: Proteins fold in a time range of microseconds to minutes despite the large amount of possible conformers. Molecular dynamics simulations of a three-stranded antiparallel beta-sheet peptide (for a total of 12.6 microsec and 72 folding events) show that at the melting temperature the unfolded state ensemble contains many more conformers than those sampled during a folding event.
authors.affiliation: Department of Biochemistry, University of Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland.
authors.forename: Andrea
authors.initials: A
authors.lastname: Cavalli
authors.forename: Urs
authors.initials: U
authors.lastname: Haberthür
authors.forename: Emanuele
authors.initials: E
authors.lastname: Paci
authors.forename: Amedeo
authors.initials: A
authors.lastname: Caflisch
mesh_terms: D000465:Algorithms; D003198:Computer Simulation; D008956:Models, Chemical; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013816:Thermodynamics; D013997:Time Factors
chemical_list: D011506:Proteins