Karle, Isabella L and Awasthi, Satish K and Balaram, Padmanabhan (1996) A designed beta-hairpin peptide in crystals. In: Proceedings of the National Academy of Sciences of the United States of America, 93 (16). pp. 8189-8193.
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 for this article belongs to National Academy of Sciences.|
|Keywords:||two conformers;octapeptides;ideal pleated sheets;beta-turn nucleating segment|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||30 Oct 2004|
|Last Modified:||19 Sep 2010 04:17|
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