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Conformational properties of methionine homo‐oligopeptides in solution
Author(s) -
Bonora Gian Maria,
Toniolo Claudio
Publication year - 1974
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1974.360131103
Subject(s) - pentamer , chemistry , oligopeptide , oligomer , methionine , helix (gastropod) , crystallography , stereochemistry , peptide , amino acid , polymer chemistry , biochemistry , ecology , snail , biology
A conformational analysis was carried out in solution on a series of L ‐methionine oligomers having the general formula \documentclass{article}\pagestyle{empty}\begin{document}$ {\rm BOC\rlap{--} (L - Met\rlap{--})}_n {\rm OMe (}n = 2 - 7)$\end{document} . We examined these oligopeptides in TFE, HFIP, EG, and mixed organic–water media. The critical size for helix formation was found to be seven residues in TFE, whereas the β‐associated structure appears at the pentamer in EG and TFE–water (20 : 80, v/v). In HFIP, however, the oligomers exist essentially in an unordered conformation.