Nair, C. M. K. ; Nagaraj, R. ; Ramaprasad, S. ; Balaram, P. ; Vijayan, M. (1981) Internal water bridge and antiparallel sheet in the structure of benzyloxycarbonyl-L-alanyl-D-phenylalanyl-L-proline monohydrate Acta Crystallographica Section B: Structural Science, 37 (3). pp. 597-601. ISSN 0108-7681
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Official URL: http://onlinelibrary.wiley.com/doi/10.1107/S056774...
Related URL: http://dx.doi.org/10.1107/S0567740881003646
Abstract
Benzyloxycarbonyl-L-alanyl-o-phenylalanyl-L-proline monohydrate, C25H29N3O6.H2O, crystallizes in the orthorhombic space group P212121 with four molecules in a unit cell of dimensions a = 9.594 (9), b = 9.705 (4) and c = 27.9 17 (12) Å. The structure has been refined to an R value of 0.067 for 2046 observed reflections. All the peptide units in the molecule are trans and the prolyl residue is in the conformation. The lone water molecule in the structure is hydrogen bonded to the carbonyl O atom in the C2 - Cγ - exo - Cβ endo conformation. The lone water molecule in the structure is hydrogen bonded to the carbonyl O atom in the benzyloxycarbonyl group and to one of the O atoms in the terminal carboxyl group. This internal water bridge, observed for the first time in a linear peptide, provides a model for water-mediated chain-reversal. An interesting feature of the crystal structure is the presence of an antiparallel sheet involving the alanyl and the phenyl-alanyl residues.
Item Type: | Article |
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Source: | Copyright of this article belongs to International Union of Crystallography. |
ID Code: | 23923 |
Deposited On: | 01 Dec 2010 12:54 |
Last Modified: | 17 May 2016 07:43 |
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