CONFORMATIONAL ANALYSIS OF THE RIGHT‐HAND TWISTED ANTIPARALLEL β‐STRUCTURE

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Abstract
The conformational analysis of a pair of 2-linked peptide units in the antiparallel arrangement is reported with a view to study the effect of association of 1 chain with the other. Tha pair of 2-linked peptide units were fixed in space through the H bonds between them in accordance with certain H bond criteria. Model building was undertaken to ascertain whether the proximity of the side-chains could be used to eliminate any 1 of the right-hand twisted, left-hand twisted or regular .beta.-structures. Stereochemically, it was possible with all of them. The preference for a right-hand twisted .beta.-structure 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 .beta.-pleated sheets present in globular proteins. The agreement between the minimum energy conformations obtained for the pair of 2-linked peptide units and the globular protein data is also indicated.