@article{
author = "Berberina, Luka and Nikolić, Milan and Stojanović, Srđan Đ. and Zlatović, Mario",
year = "2023",
abstract = "The influences of π-π 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 π-π interactions. Phenylalanine (Phe) and tyrosine (Tyr) residues were found to be involved in π–π interactions much more frequently than tryptophan (Trp) or histidine (His). Similarly, the Phe-Phe and Tyr-Tyr π–π interacting paiThe influences of π-π 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 π-π interactions. Phenylalanine (Phe) and tyrosine (Tyr) residues were found to be involved in π–π interactions much more frequently than tryptophan (Trp) or histidine (His). Similarly, the Phe-Phe and Tyr-Tyr π–π interacting pair had the highest frequency of occurrence. In addition to π-π interactions, the aromatic residues also form π-networks in phycocyanins. The π–π interactions are most favourable at the pair distance range of 5.5–7 Å, with a clear preference for T-shaped ring arrangements. Using ab initio calculations, we observed that most of the π-π interactions possess energy from 0 to -10 kJ mol-1. Stabilization centres for these proteins showed that all residues found in π-π interactions are important in locating one or more such centres. π-π 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.r had the highest frequency of occurrence. In addition to π-π interactions, the aromatic residues also form π-networks in phycocyanins. The π–π interactions are most favourable at the pair distance range of 5.5–7 Å, with a clear preference for T-shaped ring arrangements. Using ab initio calculations, we observed that most of the π-π interactions possess energy from 0 to -10 kJ mol-1. Stabilization centres for these proteins showed that all residues found in π-π interactions are important in locating one or more such centres. π-π 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.",
publisher = "Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "On the importance of π–π interactions in structural stability of phycocyanins: Scientific paper",
volume = "88",
number = "5",
pages = "481-494",
doi = "10.2298/JSC221201008B"
}