Raghavendra, K and Sasisekharan, V (1979) Conformational analysis of the right-hand twisted antiparallel β-Structure. In: International Journal of Peptide & Protein Research, 14 (4). pp. 326-338.Full text not available from this repository.
The conformational analysis of a pair of two-linked peptide units in the anti-parallel arrangement is reported here with a view to study the effect of association of one chain with the other. The pair of two-linked peptide units were fixed in space through the hydrogen bonds between them, in accordance with certain hydrogen bond criteria. Model building was undertaken to ascertain whether the proximity of the side-chains could be used to eliminate any one of the right-hand twisted, left-hand twisted or regular β-structures. Stereochemically, it was found possible with all of them. The preference for a right-hand twisted β-structure, however, was indicated by the classical energy calculations. The relevance of the results thus obtained is discussed in the context of the preferential right-hand twist of the β-pleated sheets present in globular proteins. The agreement between the minimum energy conformations obtained for the pair of two-linked peptide units and the globular protein data is also indicated.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Munksgaard int publ ltd.|
|Keywords:||antiparallel β-structure;conformational analysis;right-hand twisted β-sheets in globular proteins.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||24 Sep 2010 09:45|
|Last Modified:||24 Sep 2010 09:45|
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