Folding and unfolding of an elastinlike oligopeptide: "inverse temperature transition," reentrance, and hydrogen-bond dynamics.
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.
Schreiner
Eduard
E
Lehrstuhl für Theoretische Chemie, Ruhr-Universität Bochum, 44780 Bochum, Germany.
Nicolini
Chiara
C
Ludolph
Björn
B
Ravindra
Revanur
R
Otte
Nikolaj
N
Kohlmeyer
Axel
A
Rousseau
Roger
R
Winter
Roland
R
Marx
Dominik
D
D004549:Elastin / Q000737:chemistry*; D006860:Hydrogen Bonding; D009842:Oligopeptides / Q000737:chemistry*; D017510:Protein Folding; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature; D013816:Thermodynamics
D009842:Oligopeptides; D004549:Elastin