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X-ray conformational study of hydrazino peptide analogues.

作者信息

Aubry A, Bayeul D, Mangeot J P, Vidal J, Sterin S, Collet A, Lecoq A, Marraud M

机构信息

CNRS-URA-809, Université de Nancy I, Vandoeuvre, France.

出版信息

Biopolymers. 1991 May;31(6):793-801. doi: 10.1002/bip.360310625.

Abstract

We have solved the crystal structures of nine pseudo-peptide analogues deriving from the hydrazino analogue of glycine or valine (N beta H2-N alpha H-C alpha HR-CO2H, R = H or iPr) or proline (N beta H2-N alpha-C alpha H-CO2H) and containing the hydrazide (CO-N beta H-N alpha less than) or N beta-Z-aminoamide [formula; see text] [CO-N alpha(N beta HZ)] peptidomimetic link. This study gives access to the average geometry of these two links, to their inter- and intramolecular interaction modes, and to their influence on the conformational properties of the molecules.

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