An observation of a folded β-Ala conformation in a model peptide: Boc-L-Pip-β-Ala-NHCH3, X-ray diffraction study

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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Abstract

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.

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:	30 Jan 2012 17:58
Last Modified:	30 Jan 2012 17:58
URI:	http://crdd.osdd.net/open/id/eprint/777

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