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.
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Abstract
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 |
| URI: | http://eprints.iisc.ernet.in/id/eprint/27915 |
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A designed (3-hairpin peptide in crystals. (deposited 19 May 2010 05:01)
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