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Conformational properties of methionine homo-oligopeptides in solution

✍ Scribed by Gian Maria Bonora; Claudio Toniolo

Publisher
Wiley (John Wiley & Sons)
Year
1974
Tongue
English
Weight
561 KB
Volume
13
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

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.

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