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Conformational analysis of cyclo (l-cystine

Mitra, Alok K and Chandrasekaran, R (1977) Conformational analysis of cyclo (l-cystine. In: International Journal of Peptide and Protein Research, 10 (3). 235 -239.

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Official URL: http://www3.interscience.wiley.com/journal/1215986...


Conformational analysis of cyclo(L-cystine) shows that the diketopiperazine ring has to exist only in the boat form. With this geometry, the molecule can adopt two distinct forms differing mainly in the chirality of the disulphide bridge. In both the P- and M-models, corresponding to dihedral angles of nearly + 90° and —90° respectively about the S-S bond, the molecule displays an approximate two-fold symmetry. According to our semi-empirical energy calculations, the minimum energy of the M-model is —9.2 kcal/mol, only 0.3 kcal/mol lower than that of the P-model. Because the difference between the two minima is so small, neither form is clearly superior to the other. However, the number of low energy conformations of the M-model in the allowed conformational space is significantly larger than that of the P-model by a ratio of 3 to 1, and therefore the former is likely to be thermodynamically favoured.

Item Type: Journal Article
Publication: International Journal of Peptide and Protein Research
Publisher: Wiley
Additional Information: Copyright of this article belongs to Wiley.
Keywords: boat structure-cyclo(l-cystine;)diketopiperazine;disulphide bridge; energy calculations
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 21 Jan 2010 09:19
Last Modified: 21 Jan 2010 09:19
URI: http://eprints.iisc.ac.in/id/eprint/24350

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