ICAR Research Data Repository for Knowledge Management
Entrapping unusual folding characteristics of the beta-Ala residues in a model peptide: Boc-beta-Ala-Aib-beta-Ala-NHCH3.
DIR@IMTECH: CSIR-Institute of Microbial Technology
View Archive Info| Field | Value | |
| Title |
Entrapping unusual folding characteristics of the beta-Ala residues in a model peptide: Boc-beta-Ala-Aib-beta-Ala-NHCH3.
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| Creator |
Thakur, A K
Venugopalan, P Kishore, Raghuvansh |
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| Subject |
QD Chemistry
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| Description |
Crystal structure analysis of a model peptide: Boc-beta-Ala-Aib-beta-Ala-NHCH3 (beta-Ala: 3-amino propionic acid; Aib: alpha-aminoisobutyric acid) revealed distinct conformational preferences for folded [phi approximately 136 degrees, mu approximately -62 degrees, psi approximately 100 degrees] and semifolded [phi approximately 83 degrees, mu approximately -177 degrees, psi approximately -117 degrees] structures of the N-and C-terminus beta-Ala residues, respectively. The overall folded conformation is stabilized by unusual Ni...H-Ni+1 and nonconventional C-H...O intramolecular hydrogen bonding interactions.
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| Publisher |
Wiley
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| Date |
2000-07
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://crdd.osdd.net/open/311/1/kishore2000.3.pdf
Thakur, A K and Venugopalan, P and Kishore, Raghuvansh (2000) Entrapping unusual folding characteristics of the beta-Ala residues in a model peptide: Boc-beta-Ala-Aib-beta-Ala-NHCH3. The journal of peptide research : official journal of the American Peptide Society, 56 (1). pp. 55-8. ISSN 1397-002X |
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| Relation |
http://onlinelibrary.wiley.com/doi/10.1034/j.1399-3011.2000.00737.x/abstract
http://crdd.osdd.net/open/311/ |
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