Abstract
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)2 of -53.5(7) degrees and chi(21)1 of -55.4(8) degrees and the serine hydroxyl group has chi(1)2 of 68.2(7) degrees. The conformational angles deviate significantly from those of the 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.
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More From: The journal of peptide research : official journal of the American Peptide Society
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