title: Nanosecond folding dynamics of a three-stranded beta-sheet.
abstract: We studied conformational stability and folding kinetics of a three-stranded beta-sheet containing two rigid turns. Static infrared measurements indicate that this beta-sheet undergoes a broad but cooperative thermal unfolding transition with a midpoint at approximately 53 degrees C. Interestingly, time-resolved infrared experiments show that its relaxation kinetics in response to a temperature-jump (T-jump) occur on the nanosecond time scale (e.g., the relaxation time is approximately 140 ns at 35.0 degrees C), thereby suggesting that the conformational relaxation encounters only a small free energy barrier or even proceeds in a downhill manner. Further Langevin dynamics simulations suggest that the observed T-jump relaxation kinetics could be modeled by a conformational diffusion process along a single-well free energy profile, which allowed us to determine the effective diffusion constant and also the roughness of the folding energy landscape.
authors.affiliation: Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
authors.forename: Yao
authors.initials: Y
authors.lastname: Xu
authors.forename: Pradipta
authors.initials: P
authors.lastname: Purkayastha
authors.forename: Feng
authors.initials: F
authors.lastname: Gai
mesh_terms: D000595:Amino Acid Sequence; D031541:Fluorescence Resonance Energy Transfer; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013816:Thermodynamics
chemical_list: D009842:Oligopeptides