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
Full text not available from this repository.
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 |
Repository Staff Only: item control page