Folding and unfolding of an elastinlike oligopeptide: "inverse temperature transition," reentrance, and hydrogen-bond dynamics

Eduard Schreiner, Chiara Nicolini, Björn Ludolph, Revanur Ravindra, Nikolaj Otte, Axel Kohlmeyer, Roger Rousseau, Roland Winter, Dominik Marx

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55 Citations (Scopus)

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.

Original languageEnglish
Number of pages1
JournalPhysical review letters
Volume92
Issue number14
Publication statusPublished - Apr 9 2004

ASJC Scopus subject areas

  • Physics and Astronomy(all)

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    Schreiner, E., Nicolini, C., Ludolph, B., Ravindra, R., Otte, N., Kohlmeyer, A., Rousseau, R., Winter, R., & Marx, D. (2004). Folding and unfolding of an elastinlike oligopeptide: "inverse temperature transition," reentrance, and hydrogen-bond dynamics. Physical review letters, 92(14).