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

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

Research output: Contribution to journal › Article › peer-review

61 Scopus citations

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 language	English
Pages (from-to)	148101
Number of pages	1
Journal	Physical Review Letters
Volume	92
Issue number	14
State	Published - Apr 9 2004
Externally published	Yes

Cite this

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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.",

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T1 - Folding and unfolding of an elastinlike oligopeptide

T2 - "inverse temperature transition," reentrance, and hydrogen-bond dynamics

AU - Schreiner, Eduard

AU - Nicolini, Chiara

AU - Ludolph, Björn

AU - Ravindra, Revanur

AU - Otte, Nikolaj

AU - Kohlmeyer, Axel

AU - Rousseau, Roger

AU - Winter, Roland

AU - Marx, Dominik

PY - 2004/4/9

Y1 - 2004/4/9

N2 - 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.

AB - 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.

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M3 - Article

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SP - 148101

JO - Physical Review Letters

JF - Physical Review Letters

IS - 14

ER -

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

Abstract

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