Abstract
The influences of ?-? interactions in phycocyanin proteins and their environmental preferences were analyzed. The observations indicate that the majority of the aromatic residues in phycocyanin proteins are involved in ?-? interactions. Phenylalanine (Phe) and tyrosine (Tyr) residues were found to be involved in ??? interactions much more frequently than tryptophan (Trp) or histidine (His). Similarly, the Phe-Phe and Tyr-Tyr ?-? interacting pair had the highest frequency of occurrence. In addition to ?-? interactions, the aromatic residues also form ?-networks in phycocyanins. The ??? interactions are most favourable at the pair distance range of 5.5?7 ?, with a clear preference for T-shaped ring arrangements. Using ab initio calculations, we observed that most of the ?-? interactions possess energy from 0 to -10kJ mol-1. Stabilization centres for these proteins showed that all residues found in ?-? interactions are important in locating one or more such centres. ?-? interacting residues are evolutionary conserved. The results obtained from this study will be beneficial in further understanding the structural stability and eventual development of protein engineering of phycocyanins.
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