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Folded structures in protonated reduced dipeptides.

作者信息

Grand V, Aubry A, Dupont V, Vicherat A, Marraud M

机构信息

Laboratory of Macromolecular Physical Chemistry, ENSIC-INPL, Nancy, France.

出版信息

J Pept Sci. 1996 Nov-Dec;2(6):381-91. doi: 10.1002/psc.78.

DOI:10.1002/psc.78
PMID:9230466
Abstract

Reduced dipeptides with the general formula RCO-Xaa-rXbb-N+HR'R" (rXbb, reduced analogue of residue Xbb: NH-C alpha HR1-CrH2) are shown to adopt a folded conformation in solution and in the solid state. The protonated reduced amide bond is an active proton donor capable of interacting with a peptide carbonyl to give a strong hydrogen bond topologically equivalent to the i+2 or i+3-->i interaction. The resulting conformation is similar to the y- or beta-turn structure found in peptides and proteins.

摘要

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