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Acyclic peptides as conformational models Crystal structure of Boc-Aib-Leu-Pro-NHMe± 2H2O

Prasad, BV Venkataram and Balaram, H and Balaram, P (1984) Acyclic peptides as conformational models Crystal structure of Boc-Aib-Leu-Pro-NHMe± 2H2O. In: International journal of peptide and protein, 24 (2). pp. 135-140.

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Official URL: http://www3.interscience.wiley.com/journal/1215292...


The tripeptide Boc-Aib-Leu-Pro-NHMe crystallizes in the orthorhombic space group P212121 with a = 9.542, b = 15.200, c = 18.256 Å and Z = 4. Each peptide is associated wth two water molecules in the asymmetric unit of the crystal. The structure has been solved by direct methods and refined to an R-value of 0.069. The peptide adopts a structure without any intramolecular hydrogen bond. The three residues occupy distinctly different regions of the Ramachandran map: Aib in the left-handed 310-helical region (± = 67°, ± = 23°), Leu in the β-sheet region (± = - 133°, ± = 142°) and Pro in the poly (Pro) II region (± = - 69°, ± = 151°). An interesting observation is that each water molecule participates in four hydrogen bonds with distorted tetrahedral coordination about the oxygen atom.

Item Type: Journal Article
Publication: International journal of peptide and protein
Publisher: Wiley InterScience
Additional Information: Copyright of this article belongs to Wiley InterScience.
Keywords: α-aminoisobutyryl peptides;peptide conformation;peptide hydration;proline peptides;X-ray crystal structure
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 18 Aug 2009 04:32
Last Modified: 18 Aug 2009 04:32
URI: http://eprints.iisc.ac.in/id/eprint/22360

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