Crystallographic characterisation of novel β-turn like folds in a model peptide: stabilisation by main-chain to side-chain interactions

Thakur, A K and Kishore, Raghuvansh (2001) Crystallographic characterisation of novel β-turn like folds in a model peptide: stabilisation by main-chain to side-chain interactions. Tetrahedron Letters, 42 (28). pp. 4691-4694. ISSN 00404039

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Abstract

X-Ray diffraction analysis of the model peptide Boc-Thr-Thr-OCH3 reveals the existence of distinctive conformational characteristics: semi-extended (φ=−62.1°; ψ=137.1°) and semi-folded (φ=−130.3°; ψT=5.7°) of the N- and C-terminus Thr residues, respectively. Surprisingly, an overall significantly ‘flat’ conformation is stabilised by a number of novel main-chain to side-chain intramolecular hydrogen bonds, i.e. two non-conventional: Cγi+1H⋯OCi−1 and CγiH⋯Oi+1 types and two conventional: NiH⋯Oγi and OγiH⋯Ni types of interactions

Item Type:	Article
Additional Information:	Copyright of this article belongs to Elsevier Science.
Subjects:	Q Science > QD Chemistry
Depositing User:	Dr. K.P.S.Sengar
Date Deposited:	03 Feb 2012 05:50
Last Modified:	09 Jan 2015 11:11
URI:	http://crdd.osdd.net/open/id/eprint/863

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