Yennawar, Hemant P and Natarajan, S and Viswamitra, MA (1991) Crystal and molecular structure of l-valyl-l-lysine hydrochloride. In: International Journal of Peptide & Protein Research, 38 (6). pp. 569-573.
Full text not available from this repository. (Request a copy)Abstract
l-Valyl-l-lysine hydrochloride, C11N3O3H23 HCl, rystallizes in the monoclinic space group P2, with a = 5.438(5), b = 14.188(5), c = 9.521(5) Å, β= 95.38(2)° and Z = 2. The crystal structure, solved by direct methods, refined to R = 0.036, using full matrix least-squares method. The peptide exists in a zwitterionic form, with the N atom of the lysine side-chain protonated. The two γ-carbons of the valine side-chain have positional disorder, giving rise to two conformations, χ111= -67.3 and 65.9°, one of which (65.9°) is sterically less favourable and has been found to be less popular amongst residues branching at β-C. The lysine side-chain has the geometry of g− tgt, not seen in crystal structures of the dipeptides reported so far. Interestingly, χ32 (63.6°) of lysine side-chain has a gauche+ conformation unlike in most of the other tructures, where it is trans. The neighbouring peptide molecules are hydrogen bonded in a head-to-tail fashion, a rather uncommon interaction in lysine peptide structures. The structure shows considerable similarity with that of l-Lys-l-Val HO in conformational angles and H-bond interactions [4].
| Item Type: | Journal Article |
|---|---|
| Publication: | International Journal of Peptide & Protein Research |
| Publisher: | Munksgaard Int Publ Ltd |
| Additional Information: | Copyright of this article belongs to Munksgaard Int Publ Ltd. |
| Keywords: | Crystal structure;peptide conformation;l-Val-l-Lys. |
| Department/Centre: | Division of Physical & Mathematical Sciences > Physics |
| Date Deposited: | 16 Nov 2010 10:15 |
| Last Modified: | 16 Nov 2010 10:15 |
| URI: | http://eprints.iisc.ac.in/id/eprint/33722 |
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