International journal of peptide & protein research · 1986 · 35 citations · 27 references
Life SciencesBiochemistryBiophysicsProtein BiochemistryProtein EngineeringStructural BiologyMacromolecular StructurePeptide ChemistryProtein ConformationProtein StructureSecondary StructureSecondary Structure FormationConformational Transition StatesPeptide FoldingPeptide Secondary StructurePeptide Self-assemblyPeptide Structure AnalysisProtein Secondary Structure AnalysisProtein Self-assemblyTransition States In Conformational Changes
The conformational behaviour of the monodisperse amphiphilic oligopeptides (L‐Thr‐L‐Val) n (I and II) and (L‐Ser‐L‐Leu) n (III) for n = 1–4 was investigated by CD spectroscopy in TFE, MeOH and water. A conformational transition random‐coil ‐> ß‐structure was observed for both series: the critical chain length for ß‐structure formation turned out to be dependent on solvent and spatial similarity of the amino acid side‐chains. The very short critical chain‐length for the onset of ß‐structure formation for peptides I and II (n = 3) is explained by the formation of bilayer sheets, in which the minimization of hydrophobic contacts between the amphipilic peptide and the hydrophilic solvent represents an important driving force for ß‐structure formation. The use of amphiphilic peptides for the construction of artificial proteins is briefly discussed.
27