Prasad, S. ; Mitra, S. ; Subramanian, E. ; Velmurugan, D. ; Rao, R. B. ; Balaram, P. (1994) Coexistence of folded and extended conformations of a tripeptide containing α,α-di-n-propylglycine in crystals Biochemical and Biophysical Research Communications, 198 (2). pp. 424-430. ISSN 0006-291X
Full text not available from this repository.
Official URL: http://linkinghub.elsevier.com/retrieve/pii/S00062...
Related URL: http://dx.doi.org/10.1006/bbrc.1994.1062
Abstract
The crystal structure of the tripeptide Boc-Leu-Dpg-Val-OMe (Dpg, α,α-di-n-propylglycine) reveals the coexistence of two distinct backbone conformations. In molecule A the Dpg residue adopts a fully extended conformation (φ = 76.0°, ψ =180.0°) while in molecule B a left handed helical conformation (φ = 62.8°, ψ = 39.6°) is observed. Molecule B adopts a folded structure corresponding to a highly distorted Type II β-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: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier Science. |
| ID Code: | 4475 |
| Deposited On: | 18 Oct 2010 07:45 |
| Last Modified: | 16 May 2011 06:29 |
Repository Staff Only: item control page
