Prasad, S and Mitra, S and Subramanian, E and Velmurugan, D and Rao, RB and Balaram, P (1994) Coexistence of Folded and Extended Conformations of a Tripeptide Containing alpha,alpha-Di-n-propylglycine in Crystals. In: Biochemical and Biophysical Research Communications, 198 (2). pp. 424-430.
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Abstract
The crystal structure of the tripeptide Boc-Leu-Dpg-Val-OMe (Dpg, alpha, alpha-di-n-propylglycine) reveals the coexistence of two distinct backbone conformations. In molecule A the Dpg residue adopts a fully extended conformation (phi = 76.0°, psi=180.0°) while in molecule B a left handed helical conformation (phi = 62.8°, psi= 39.6°) is observed. Molecule B adopts a folded structure corresponding to a highly distorted Type II beta-turn conformation, which lacks an intramolecular 4 → 1 hydrogen bond. In contrast, molecule A has an open, extended conformation. The results demonstrate that both fully extended and helical conformations are energetically accessible to the Dpg residue.
Item Type: | Journal Article |
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Publication: | Biochemical and Biophysical Research Communications |
Publisher: | Academic Press |
Additional Information: | Copyright for this article belongs to Academic Press. |
Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
Date Deposited: | 11 Nov 2004 |
Last Modified: | 17 Jan 2012 09:57 |
URI: | http://eprints.iisc.ac.in/id/eprint/2317 |
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