6533b7ddfe1ef96bd12753ff
RESEARCH PRODUCT
Conformational characteristics of homo-oligopeptides of O-benzyl-L-tyrosine+
Hermann AnzingerM. MutterV. MorettoClaudio TonioloGian Maria Bonorasubject
chemistry.chemical_classificationCircular dichroismChemical PhenomenaSpectrophotometry InfraredBase (chemistry)Protein ConformationStereochemistryHydrogen bondCircular DichroismInfrared spectroscopyBiochemistryPeptide ConformationSolutionsSolventChemistrychemistry.chemical_compoundchemistryTyrosineAbsorption (chemistry)OligopeptidesDerivative (chemistry)description
Conformational studies of X[-L-Tyr(Bzl)-]n-series bound to polyethyleneglycol (X = H2, Nps; n = 3-8) in the solid state and in solvents of different polarities and capabilities of forming hydrogen bonds are reported. By using i.r. absorption, the occurrence of the beta-structure in the higher oligomers in the solid state was established. By means of i.r. absorption and CD the onset of that ordered conformation in solution was assessed as a function of chain length. The effects induced by the presence of the N-protecting group and added base, and by changing the nature of solvent on the conformational preferences of the [-L-Tyr(Bzl)-]n homo-peptides were also examined. The 2-nitrophenylsulphenyl chromophoric derivative of the alpha-amino group is proposed as a circular dichroism sensor for beta-structure in peptides.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1983-04-01 | International Journal of Peptide and Protein Research |