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Protein Science, Vol 7, Issue 2 383-388, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

Trifluoroethanol effects on helix propensity and electrostatic interactions in the helical peptide from ribonuclease T(1)

J. K. MYERS, C. N. PACE and J. M. SCHOLTZ
Present address: Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710.

Trifluoroethanol (TFE) is often used to increase the helicity of peptides to make them usable as models of helices in proteins. We have measured helix propensities for all 20 amino acids in water and two concentrations of trifluoroethanol, 15 and 40% (v/v) using, as a model system, a peptide derived from the sequence of the {alpha}-helix of ribonuclease T(1). There are three main conclusions from our studies. (1) TFE alters electrostatic interactions in the ribonuclease T(1) helical peptide such that the dependence of the helical content on pH is lost in 40% TFE. (2) Helix propensities measured in 15% TFE correlate well with propensities measured in water, however, the correlation with propensities measured in 40% TFE is significantly worse. (3) Propensities measured in alanine-based peptides and the ribonuclease T(1) peptide in TFE show very poor agreement, revealing that TFE greatly increases the effect of sequence context.
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