Entropy calculations on a reversibly folding peptide: Changes in solute free energy cannot explain folding behavior

Schafer, H., Daura, X., Mark, A. E. and van Gunsteren, W. F. (2001) Entropy calculations on a reversibly folding peptide: Changes in solute free energy cannot explain folding behavior. Proteins-structure Function And Genetics, 43 1: 45-56. doi:10.1002/1097-0134(20010401)43:1<45::AID-PROT1016>3.0.CO;2-N


Author Schafer, H.
Daura, X.
Mark, A. E.
van Gunsteren, W. F.
Title Entropy calculations on a reversibly folding peptide: Changes in solute free energy cannot explain folding behavior
Journal name Proteins-structure Function And Genetics   Check publisher's open access policy
ISSN 0887-3585
Publication date 2001-01-01
Sub-type Article (original research)
DOI 10.1002/1097-0134(20010401)43:1<45::AID-PROT1016>3.0.CO;2-N
Volume 43
Issue 1
Start page 45
End page 56
Total pages 12
Place of publication New York
Publisher Wiley-liss
Language eng
Abstract The configurational entropy of a beta -heptapeptide in solution at four different temperatures is calculated, The contributions of the backbone and of the side-chain atoms to the total peptide entropy are analyzed separately and the effective contribution to the entropy arising from correlations between these terms determined. The correlation between the backbone and side-chain atoms amounts to about 17% and is rather insensitive to the temperature. The correlation of motion within the backbone and within side-chains is much larger and decreases with temperature. As the peptide reversibly folds at higher temperatures, its change in entropy and enthalpy upon folding is analyzed. The change in entropy and enthalpy upon folding of the peptide alone cannot account for the observed change in free energy on folding of the peptide in solution. Enthalpic and entropic contributions of the solvent thus also play a key role. Proteins 2001; 43:45-56. (C) 2001 Wiley Liss, Inc.
Keyword Biochemistry & Molecular Biology
Biophysics
Molecular-dynamics Simulation
Conformational Entropy
Secondary Structure
Protein
Macromolecules
Absolute
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
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Created: Thu, 20 Sep 2007, 02:19:19 EST