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Hydrophobic solvation in aqueous trifluoroethanol solution
Author(s) -
Bodkin Michael J.,
Goodfellow Julia M.
Publication year - 1996
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(199607)39:1<43::aid-bip5>3.0.co;2-v
Subject(s) - chemistry , aqueous solution , solvation , molecule , solvent , side chain , helix (gastropod) , hydrophobic effect , solvation shell , peptide , crystallography , organic chemistry , polymer , ecology , biochemistry , snail , biology
The titration of an aqueous solution of a de novo designed peptide with trifluoroethanol (TFE) shows complete helix formation with the addition of only 30% TFE. A molecular simulation of the peptide, in which a single shell of TFE molecules initially surrounds the peptide, reveals preferred sites of solvent interaction. The TFE molecules show greater preference for the hydrophobic compared with hydrophilic side chains. The helix‐enhancing ability of TFE in aqueous solution may be rationalized in terms of stabilizing the hydrophobic collapse of apolar side chains of the formed helix. © 1996 John Wiley & Sons, Inc.