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An observation of a folded β-Ala conformation in a model peptide: Boc-L-Pip-β-Ala-NHCH3, X-ray diffraction study
DIR@IMTECH: CSIR-Institute of Microbial Technology
View Archive Info| Field | Value | |
| Title |
An observation of a folded β-Ala conformation in a model peptide: Boc-L-Pip-β-Ala-NHCH3, X-ray diffraction study
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| Creator |
Thakur, Ashwani K.
Kishore, Raghuvansh |
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| Subject |
QD Chemistry
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| Description |
An X-ray crystallographic characterization of a ‘locally folded’ conformation of a β-Ala residue, in a short linear peptide: Boc-L-Pip-β-Ala-NHCH3, has been described. The critical μ torsion angle between the methylene groups of the β-Ala adopts a typical gauche (g−) conformation. The urethane moiety is found in the uncommon type a. The influence of the geometrical variation of the Pip residue on β-Ala conformation has been emphasized.
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| Publisher |
Elsevier Science/Academic Press
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| Date |
1998
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://crdd.osdd.net/open/777/1/kishore1998.pdf
Thakur, Ashwani K. and Kishore, Raghuvansh (1998) An observation of a folded β-Ala conformation in a model peptide: Boc-L-Pip-β-Ala-NHCH3, X-ray diffraction study. Tetrahedron Letters, 39 (51). pp. 9553-9556. ISSN 00404039 |
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| Relation |
http://dx.doi.org/10.1016/S0040-4039(98)02122-4
http://crdd.osdd.net/open/777/ |
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