Conformational characteristics of homo-oligopeptides of O-benzyl-L-tyrosine

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 oligom...

Full description

Saved in:
Bibliographic Details
Published inInternational journal of peptide and protein research Vol. 21; no. 4; p. 336
Main Authors Bonora, G M, Moretto, V, Toniolo, C, Anzinger, H, Mutter, M
Format Journal Article
LanguageEnglish
Published Denmark 01.04.1983
Subjects
Chemical Phenomena
Chemistry
Circular Dichroism
Oligopeptides - chemical synthesis
Protein Conformation
Solutions
Spectrophotometry, Infrared
Tyrosine - analogs & derivatives
Online AccessGet more information

Cover

More Information
Summary: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.
ISSN:0367-8377
DOI:10.1111/j.1399-3011.1983.tb03113.x