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

✍ Scribed by A.K Thakur; R Kishore

Publisher: Elsevier Science
Year: 2001
Tongue: French
Weight: 84 KB
Volume: 42
Category: Article
ISSN: 0040-4039
DOI: 10.1016/s0040-4039(01)00788-2

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✦ Synopsis

X-Ray diffraction analysis of the model peptide Boc-Thr-Thr-OCH 3 reveals the existence of distinctive conformational characteristics: semi-extended (=-62.1°; =137.1°) and semi-folded (=-130.3°; T =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: