Venkataram Prasad, B. V. ; Balaram, H. ; Balaram, P. (1984) Acyclic peptides as conformational models. Crystal structure of Boc-Aib-Leu-Pro-NHMe ±2H2O International Journal of Peptide and Protein Research, 24 (2). pp. 135-140. ISSN 0367-8377
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Official URL: http://www3.interscience.wiley.com/journal/1215292...
Related URL: http://dx.doi.org/10.1111/j.1399-3011.1984.tb00938.x
Abstract
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: | Article |
|---|---|
| Source: | Copyright of this article belongs to Munksgaard International Publishers. |
| Keywords: | α-aminoisobutyryl Peptides; Peptide Conformation; Peptide Hydration; Proline Peptides; X-ray Crystal Structure |
| ID Code: | 5009 |
| Deposited On: | 18 Oct 2010 05:34 |
| Last Modified: | 14 Jun 2011 11:11 |
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