Padiyar, GS (1998) Crystal and molecular structure of L-histidyl-L-serine trihydrate: occurrence of C-alpha-H - O=C hydrogen bond motif similar to the motif in collagen triple helix and beta-sheets. In: Journal of Peptide Research, 51 (4). pp. 266-270.
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L-Histidyl-L-serine (HSN) trihydrate, C9H14N4O4 . H2O, crystallizes in the orthorhombic space group P2(1)2(1)2(1) with a = 4.865(4), b = 15.604(4), c = 18.918(5) and Z = 4. The crystal structure was solved by direct methods and refined to R1 = 0.070 by a full-matrix least-squares method. The peptide exists in a zwitterionic form, with the N-terminus in a protonated form and the C-terminus in an ionized form. The imidazole ring of histidine in its neutral His(epsilon) tautomeric state has conformational angles chi(1)(1) of -53.5(7)degrees and chi(1)(21) of -55.4(8)degrees and the serine hydroxyl group has chi(2)(1) of 68.2(7)degrees. The conformational angles deviate significantly from those or rue dipeptide complexed with glycyl-L-glutamic acid in which the histidine is protonated. A noteworthy feature of the crystal packing is the occurrence of a C-alpha-H O=C hydrogen bond motif similar to that observed in collagen triple helix and beta-sheets.
| Item Type: | Journal Article |
|---|---|
| Publication: | Journal of Peptide Research |
| Publisher: | Munksgaard International Publishers Ltd |
| Additional Information: | Copyright of this article belongs to Munksgaard International Publishers Ltd. |
| Keywords: | crystal structure;conformation;hydrogen bond;histidine. |
| Department/Centre: | Division of Physical & Mathematical Sciences > Physics |
| Date Deposited: | 11 May 2009 08:39 |
| Last Modified: | 11 May 2009 08:39 |
| URI: | http://eprints.iisc.ac.in/id/eprint/18344 |
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