ICAR Research Data Repository for Knowledge Management
Crystallographic characterisation of novel β-turn like folds in a model peptide: stabilisation by main-chain to side-chain interactions
DIR@IMTECH: CSIR-Institute of Microbial Technology
View Archive Info| Field | Value | |
| Title |
Crystallographic characterisation of novel β-turn like folds in a model peptide: stabilisation by main-chain to side-chain interactions
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| Creator |
Thakur, A K
Kishore, Raghuvansh |
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| Subject |
QD Chemistry
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| Description |
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+1H⋯OCi−1 and CγiH⋯Oi+1 types and two conventional: NiH⋯Oγi and OγiH⋯Ni types of interactions
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| Publisher |
Elsevier Science
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| Date |
2001
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://crdd.osdd.net/open/863/1/kishore2001.pdf
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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| Relation |
http://dx.doi.org/10.1016/S0040-4039(01)00788-2
http://crdd.osdd.net/open/863/ |
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