Effect of hexafluoroisopropanol on the thermodynamics of peptide secondary structure formation
This report provides additional evidence for the importance of hydrophobic interactions in peptide secondary structure formation. For the hydrophobically driven {beta} hairpin formation examined, the addition of HFIP to the 8% level increases hairpin formation and increases {Delta}C{sub p} by nearly a factor of 3. Surprisingly, {alpha} helices bearing a few non-interacting hydrophobic residues can display even larger {Delta}C{sub p} values. The initial phase of secondary structure induction during fluoroalcohol titrations of peptides appears to be largely the result of these effects rather than differential stabilization (or destabilization) of the folded versus coil conformation by alcohol/peptide binding interactions, as the latter would be reflected predominantly in the enthalpy term. The addition of limited quantities of fluoroalcohol may mimic the early hydrophobic collapse stage of protein folding.
- Research Organization:
- Univ. of Washington, Seattle, WA (US)
- Sponsoring Organization:
- National Institutes of Health (NIH)
- OSTI ID:
- 20013677
- Journal Information:
- Journal of the American Chemical Society, Vol. 121, Issue 42; Other Information: PBD: 27 Oct 1999; ISSN 0002-7863
- Country of Publication:
- United States
- Language:
- English
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