title: Infrared temperature-jump study of the folding dynamics of alpha-helices and beta-hairpins.
abstract: The laser-induced temperature-jump (T-jump) technique in conjunction with infrared spectroscopy provides a versatile means to study the early events in protein folding. Compared with the commonly used stopped-flow kinetic methods, the T-jump initiation technique offers a faster time resolution. It allows the study of protein folding processes occurring on the nanosecond-to-microsecond time-scales. In addition, infrared spectroscopy is a powerful tool for characterizing backbone conformation and dynamics. In this chapter, we mainly discuss the application of this technique to the study of the helix-coil transition dynamics and the mechanism of beta-hairpin formation.
authors.affiliation: Department of Chemistry, University of Pennsylvania, Philadelphia, USA.
authors.forename: Feng
authors.initials: F
authors.lastname: Gai
authors.forename: Deguo
authors.initials: D
authors.lastname: Du
authors.forename: Yao
authors.initials: Y
authors.lastname: Xu
mesh_terms: D000595:Amino Acid Sequence; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D007700:Kinetics; D007834:Lasers; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D013055:Spectrophotometry, Infrared; D013696:Temperature
chemical_list: D010455:Peptides