Conformational heterogeneity of tripeptides containing Boc–Leu–Aib as corner residues in the solid state

Haldar, Debasish ; Drew, Michael G. B. ; Banerjee, Arindam (2007) Conformational heterogeneity of tripeptides containing Boc–Leu–Aib as corner residues in the solid state Tetrahedron, 63 (25). pp. 5561-5566. ISSN 0040-4020

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Official URL: http://www.sciencedirect.com/science/article/pii/S...

Related URL: http://dx.doi.org/10.1016/j.tet.2007.04.026

Abstract

A critical analysis of single crystal X-ray diffraction studies on a series of terminally protected tripeptides containing a centrally positioned Aib (α-aminoisobutyric acid) residue has been reported. For the tripeptide series containing Boc–Ala–Aib as corner residues, all the reported peptides formed distorted type II β-turn structures. Moreover, a series of Phe substituted analogues (tripeptides with Boc–Phe–Aib) have also shown different β-turn conformations. However, the Leu-modified analogues (tripeptides with Boc–Leu–Aib) disrupt the concept of β-turn formation and adopt various conformations in the solid state. X-ray crystallography sheds some light on the conformational heterogeneity at atomic resolution.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:β-Turn; S-shape Structure; Conformational Heterogeneity; Tripeptides; X-Ray Crystallography.
ID Code:99615
Deposited On:04 Nov 2016 12:21
Last Modified:04 Nov 2016 12:21

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