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Structural flexibility of Aib-containing peptides: the N-terminal tripeptide of trichotoxin.

作者信息

Gessmann R, Brueckner H, Kokkinidis M

机构信息

Dept. of Biology, University of Crete, Greece.

出版信息

Biochem Biophys Res Commun. 1991 Jan 31;174(2):878-84. doi: 10.1016/0006-291x(91)91499-3.

Abstract

The sequence Aib-Gly-Aib which corresponds to the N-terminus of the microheterogeneous peptide antibiotic trichotoxin has been studied crystallographically in the context of different protecting groups. Peptides Ac-Aib-Gly-Aib-OH (A) and Z-Aib-Gly-Aib-OH (B) form beta-turns. Both peptides show a remarkable conformational flexibility forming a large variety of beta-turns of different types.

摘要

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