Stabilization of helical domains in short peptides using hydrophobic interactions.
The contribution of hydrophobic interactions in the stabilization of helical structure was compared for a series of short peptides that incorporated two epsilon-(3,5-dinitrobenzoyl)Lys residues at various positions. Results showed that in aqueous/organic mixtures, methanol induced helical stability over a wider range and at higher concentration than trifluoroethanol (TFE); a similar degree of stability was seen in low mole fraction mixtures of TFE in water. Solvent mixture titrations in TFE/water demonstrated that helical stability was highest for the peptide having a pair of modified residues spaced by three other residues. Solvent mixture titrations in TFE/water appear to be useful in indicating the degree of hydrophobic stabilization.
Albert
J S
JS
Department of Chemistry, University of Pittsburgh, Pennsylvania 15260.
Hamilton
A D
AD
D000595:Amino Acid Sequence; D066298:In Vitro Techniques; D000432:Methanol / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012995:Solubility; D012997:Solvents; D013816:Thermodynamics; D014270:Trifluoroethanol / Q000737:chemistry; D014867:Water / Q000737:chemistry
D010455:Peptides; D012997:Solvents; D014867:Water; D014270:Trifluoroethanol; D000432:Methanol