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- W2134925852 abstract "The effects of trifluoroethanol (TFE) on the stability of the α-helix formed by ribonuclease S-peptide, residues 1–19 of ribonuclease A, were studied by measuring circular dichroism as a function of TFE concentration, pH, and temperature. The S-peptide forms an unusually stable α-helix, which is known to be stabilized by TFE. The magnitude of the effect of charged groups on the peptide, manifested by the change in α-helix stability as a function of pH, was not altered significantly by either TFE concentration or temperature, indicating that the lower dielectric constant of TFE is not important in the stabilization of this α-helix. This suggests that the α-helix might be stabilized by many interactions in addition to the effects of charges. The titration curve of circular dichroism vs. TFE concentration appears to be cooperative at 0°C, but becomes progressively less cooperative at temperatures between 25 and 75°C. The properties of the TFE stabilization indicate that TFE might be a useful probe with which to measure the stability of marginally stable peptides and small proteins." @default.
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- W2134925852 date "1986-03-01" @default.
- W2134925852 modified "2023-10-14" @default.
- W2134925852 title "Stabilization of the ribonuclease S-peptide α-helix by trifluoroethanol" @default.
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- W2134925852 doi "https://doi.org/10.1002/prot.340010303" @default.
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