Abstract
A joint experimental/theoretical investigation of the elastin-like octapeptide GVG(VPGVG) was carried out. In this article a comprehensive molecular-dynamics study of the temperature-dependent folding and unfolding of the octapeptide is presented. The current study, as well as its experimental counterpart (see companion article in this issue) find that this peptide undergoes an inverse temperature transition (ITT), leading to a folding at ∼40-60°C. In addition, an unfolding transition is identified at unusually high temperatures approaching the normal boiling point of water. Due to the small size of the system, two broad temperature regimes are found: The ITT regime at ∼10-60°C and the unfolding regime at ∼ T > 60°C, where the peptide has a maximum probability of being folded at T ≈ 60°C. A detailed molecular picture involving a thermodynamic order parameter, or reaction coordinate, for this process is presented along with a time-correlation function analysis of the hydrogenbond dynamics within the peptide as well as between the peptide and solvating water molecules. Correlation with experimental evidence and ramifications on the properties of elastin are discussed.
| Original language | English |
|---|---|
| Pages (from-to) | 1393-1407 |
| Number of pages | 15 |
| Journal | Biophysical Journal |
| Volume | 86 |
| Issue number | 3 |
| Publication status | Published - Mar 2004 |
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ASJC Scopus subject areas
- Biophysics
Cite this
Temperature-Dependent Conformational Transitions and Hydrogen-Bond Dynamics of the Elastin-Like Octapeptide GVG(VPGVG) : A Molecular-Dynamics Study. / Rousseau, Roger; Schreiner, Eduard; Kohlmeyer, Axel; Marx, Dominik.
In: Biophysical Journal, Vol. 86, No. 3, 03.2004, p. 1393-1407.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Temperature-Dependent Conformational Transitions and Hydrogen-Bond Dynamics of the Elastin-Like Octapeptide GVG(VPGVG)
T2 - A Molecular-Dynamics Study
AU - Rousseau, Roger
AU - Schreiner, Eduard
AU - Kohlmeyer, Axel
AU - Marx, Dominik
PY - 2004/3
Y1 - 2004/3
N2 - A joint experimental/theoretical investigation of the elastin-like octapeptide GVG(VPGVG) was carried out. In this article a comprehensive molecular-dynamics study of the temperature-dependent folding and unfolding of the octapeptide is presented. The current study, as well as its experimental counterpart (see companion article in this issue) find that this peptide undergoes an inverse temperature transition (ITT), leading to a folding at ∼40-60°C. In addition, an unfolding transition is identified at unusually high temperatures approaching the normal boiling point of water. Due to the small size of the system, two broad temperature regimes are found: The ITT regime at ∼10-60°C and the unfolding regime at ∼ T > 60°C, where the peptide has a maximum probability of being folded at T ≈ 60°C. A detailed molecular picture involving a thermodynamic order parameter, or reaction coordinate, for this process is presented along with a time-correlation function analysis of the hydrogenbond dynamics within the peptide as well as between the peptide and solvating water molecules. Correlation with experimental evidence and ramifications on the properties of elastin are discussed.
AB - A joint experimental/theoretical investigation of the elastin-like octapeptide GVG(VPGVG) was carried out. In this article a comprehensive molecular-dynamics study of the temperature-dependent folding and unfolding of the octapeptide is presented. The current study, as well as its experimental counterpart (see companion article in this issue) find that this peptide undergoes an inverse temperature transition (ITT), leading to a folding at ∼40-60°C. In addition, an unfolding transition is identified at unusually high temperatures approaching the normal boiling point of water. Due to the small size of the system, two broad temperature regimes are found: The ITT regime at ∼10-60°C and the unfolding regime at ∼ T > 60°C, where the peptide has a maximum probability of being folded at T ≈ 60°C. A detailed molecular picture involving a thermodynamic order parameter, or reaction coordinate, for this process is presented along with a time-correlation function analysis of the hydrogenbond dynamics within the peptide as well as between the peptide and solvating water molecules. Correlation with experimental evidence and ramifications on the properties of elastin are discussed.
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UR - http://www.scopus.com/inward/citedby.url?scp=1542375359&partnerID=8YFLogxK
M3 - Article
VL - 86
SP - 1393
EP - 1407
JO - Biophysical Journal
JF - Biophysical Journal
SN - 0006-3495
IS - 3
ER -