Karle, IL and Awasthi, SK and Balaram, P (1996) A designed (3-hairpin peptide in crystals. In: Proc Natl Acad Sci Unit States Am, 93 (16). pp. 8189-8193.
This is the latest version of this item.
Restricted to Registered users only
Download (791Kb) | Request a copy
Beta-hairpin structures have been crystallographically characterized only in very short acyclic peptides, in contrast to helices. The structure of the designed beta-hairpin, t-butoxycarbonyl-Leu-Val-Val-D-Pro-Gly-Leu-Val-Val-OMe in crystals is described. The two independent molecules of the octapeptide fold into almost ideal beta-hairpin conformations with the central D-Pro-Gly segment adopting a Type II' beta-turn conformation. The definitive characterization of a beta-hairpin has implications for de novo peptide and protein design, particularly for the development of three- and four-stranded beta-sheets.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to National Academy of Sciences.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||19 May 2010 06:10|
|Last Modified:||13 Apr 2011 06:32|
Available Versions of this Item
A designed (3-hairpin peptide in crystals. (deposited 19 May 2010 05:01)
- A designed (3-hairpin peptide in crystals. (deposited 19 May 2010 06:10) [Currently Displayed]
Actions (login required)