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 |
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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 |