Rathore, Ravindranath Singh (2005) Crystal structure and conformational analyses of a synthetic tetrapeptide t-Boc-L-Val-Aib-Gly-L-Leu-OMe. In: Crystal Research and Technology, 40 (6). pp. 627-632.Full text not available from this repository. (Request a copy)
Crystal structure of a terminally blocked synthetic peptide,t-Boc-L-Val-Aib-Gly-L-Leu-OMe has been investigated. Two different conformers of peptide with one co-crystallized water molecule, coexist in the crystal structure, in C2 space group. Both the conformers are stabilized by two intramolecular 1 <- 4 hydrogen bonds, between (Boc)C=O... HN (Gly) and (Val) C=O... HN (Leu), forming consecutive typeII-I' beta-turns. In the crystal, water interlinks peptide molecules,making a triangular bridge of pyramidal type.
|Item Type:||Journal Article|
|Additional Information:||Copyright for this article belongs to John Wiley and Sons.|
|Department/Centre:||Division of Physical & Mathematical Sciences > Physics|
|Date Deposited:||12 Aug 2005|
|Last Modified:||08 Feb 2012 04:39|
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