title: Folding and unfolding of an elastinlike oligopeptide: "inverse temperature transition," reentrance, and hydrogen-bond dynamics.
abstract: The temperature-dependent behavior of a solvated oligopeptide, GVG(VPGVG), is investigated. Spectroscopic measurements, thermodynamic measurements, and molecular dynamics simulations find that this elastinlike octapeptide behaves as a two-state system that undergoes an "inverse temperature" folding transition and reentrant unfolding close to the boiling point of water. A molecular picture of these processes is presented, emphasizing changes in the dynamics of hydrogen bonding at the protein/water interface and peptide backbone librational entropy.
authors.affiliation: Lehrstuhl für Theoretische Chemie, Ruhr-Universität Bochum, 44780 Bochum, Germany.
authors.forename: Eduard
authors.initials: E
authors.lastname: Schreiner
authors.forename: Chiara
authors.initials: C
authors.lastname: Nicolini
authors.forename: Björn
authors.initials: B
authors.lastname: Ludolph
authors.forename: Revanur
authors.initials: R
authors.lastname: Ravindra
authors.forename: Nikolaj
authors.initials: N
authors.lastname: Otte
authors.forename: Axel
authors.initials: A
authors.lastname: Kohlmeyer
authors.forename: Roger
authors.initials: R
authors.lastname: Rousseau
authors.forename: Roland
authors.initials: R
authors.lastname: Winter
authors.forename: Dominik
authors.initials: D
authors.lastname: Marx
mesh_terms: D004549:Elastin / Q000737:chemistry*; D006860:Hydrogen Bonding; D009842:Oligopeptides / Q000737:chemistry*; D017510:Protein Folding; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature; D013816:Thermodynamics
chemical_list: D009842:Oligopeptides; D004549:Elastin