title: Protein folding studied by single-molecule FRET.
abstract: A complete understanding of a protein-folding mechanism requires description of the distribution of microscopic pathways that connect the folded and unfolded states. This distribution can, in principle, be described by computer simulations and theoretical models of protein folding, but is hidden in conventional experiments on large ensembles of molecules because only average properties are measured. A long-term goal of single-molecule fluorescence studies is to time-resolve the structural events as individual molecules make transitions between folded and unfolded states. Although such studies are still in their infancy, the work till now shows great promise and has already produced novel and important information on current issues in protein folding that has been impossible or difficult to obtain from ensemble measurements.
authors.affiliation: Biochemisches Institut, Universität Zürich, Winterthurerstr. 190, 8057 Zürich, Switzerland. schuler@bioc.uzh.ch
authors.forename: Benjamin
authors.initials: B
authors.lastname: Schuler
authors.forename: William A
authors.initials: WA
authors.lastname: Eaton
mesh_terms: D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry
chemical_list: D011506:Proteins