title: Submillisecond kinetics of protein folding.
abstract: New experimental methods permit observation of protein folding and unfolding on the previously inaccessible nanosecond-microsecond timescale. These studies are beginning to establish times for the elementary motions in protein folding - secondary structure and loop formation, local hydrophobic collapse, and global collapse to the compact denatured state. They permit an estimate of about one microsecond for the shortest time in which a protein can possibly fold.
authors.affiliation: Laboratory of Chemical Physics, Building 5, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA. eaton@helix.nih.gov
authors.forename: W A
authors.initials: WA
authors.lastname: Eaton
authors.forename: V
authors.initials: V
authors.lastname: Muñoz
authors.forename: P A
authors.initials: PA
authors.lastname: Thompson
authors.forename: C K
authors.initials: CK
authors.lastname: Chan
authors.forename: J
authors.initials: J
authors.lastname: Hofrichter
mesh_terms: D006801:Humans; D007700:Kinetics; D017510:Protein Folding; D017433:Protein Structure, Secondary