TY  - JOUR
AU  - Berberina, Luka
AU  - Nikolić, Milan
AU  - Stojanović, Srđan Đ.
AU  - Zlatović, Mario
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6269
AB  - 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.
PB  - Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - On the importance of π–π interactions in structural stability of phycocyanins: Scientific paper
VL  - 88
IS  - 5
SP  - 481
EP  - 494
DO  - 10.2298/JSC221201008B
ER  - 

@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"
}

Berberina, L., Nikolić, M., Stojanović, S. Đ.,& Zlatović, M.. (2023). On the importance of π–π interactions in structural stability of phycocyanins: Scientific paper. in Journal of the Serbian Chemical Society
Serbian Chemical Society., 88(5), 481-494.
https://doi.org/10.2298/JSC221201008B

Berberina L, Nikolić M, Stojanović SĐ, Zlatović M. On the importance of π–π interactions in structural stability of phycocyanins: Scientific paper. in Journal of the Serbian Chemical Society. 2023;88(5):481-494.
doi:10.2298/JSC221201008B .

Berberina, Luka, Nikolić, Milan, Stojanović, Srđan Đ., Zlatović, Mario, "On the importance of π–π interactions in structural stability of phycocyanins: Scientific paper" in Journal of the Serbian Chemical Society, 88, no. 5 (2023):481-494,
https://doi.org/10.2298/JSC221201008B . .

TY  - JOUR
AU  - Berberina, Luka
AU  - Nikolić, Milan
AU  - Stojanović, Srđan Đ.
AU  - Zlatović, Mario
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5864
AB  - The influences of cation-π interactions in phycocyanin proteins and their environmental preferences were analyzed. The number of interactions formed by arginine showed to be higher than those formed by the lysine in the cationic group, while histidine is comparatively higher than phenylalanine and N-terminal residue in the π group. Arg-Tyr and Arg-Phe interacting pairs are predominant among the various pairs analyzed. Cation-π interactions are distance-dependent and can be realized above a wider area above the π ring. We analyzed the energy contribution resulting from cation-π interactions using ab initio calculations. The energy contribution
resulting from the most frequent cation-π interactions was in the lower range of strong hydrogen bonds. The results showed that, while most of their interaction energies lay ranged from -2 to -8 kcal/mol, those energies could be up to -12 - 12 kcal/mol. Stabilization centers for these proteins showed that all residues found in cation-π interactions are important in locating one or more of such centers. In the cation–π interacting residues, 54% of the amino acid residues involved in these interactions might be conserved in phycocyanins. From this study, we infer that cation-π forming residues play an important role in the stability of the multiply commercially used phycocyanin proteins and could help structural biologists and medicinal chemists to design better and safer drugs.
PB  - Elsevier
T2  - Computational Biology and Chemistry
T1  - Influence of cation−π interactions to the structural stability of phycocyanin proteins: A computational study.
VL  - 100
SP  - 107752
DO  - 10.1016/j.compbiolchem.2022.107752
ER  - 

@article{
author = "Berberina, Luka and Nikolić, Milan and Stojanović, Srđan Đ. and Zlatović, Mario",
year = "2022",
abstract = "The influences of cation-π interactions in phycocyanin proteins and their environmental preferences were analyzed. The number of interactions formed by arginine showed to be higher than those formed by the lysine in the cationic group, while histidine is comparatively higher than phenylalanine and N-terminal residue in the π group. Arg-Tyr and Arg-Phe interacting pairs are predominant among the various pairs analyzed. Cation-π interactions are distance-dependent and can be realized above a wider area above the π ring. We analyzed the energy contribution resulting from cation-π interactions using ab initio calculations. The energy contribution
resulting from the most frequent cation-π interactions was in the lower range of strong hydrogen bonds. The results showed that, while most of their interaction energies lay ranged from -2 to -8 kcal/mol, those energies could be up to -12 - 12 kcal/mol. Stabilization centers for these proteins showed that all residues found in cation-π interactions are important in locating one or more of such centers. In the cation–π interacting residues, 54% of the amino acid residues involved in these interactions might be conserved in phycocyanins. From this study, we infer that cation-π forming residues play an important role in the stability of the multiply commercially used phycocyanin proteins and could help structural biologists and medicinal chemists to design better and safer drugs.",
publisher = "Elsevier",
journal = "Computational Biology and Chemistry",
title = "Influence of cation−π interactions to the structural stability of phycocyanin proteins: A computational study.",
volume = "100",
pages = "107752",
doi = "10.1016/j.compbiolchem.2022.107752"
}

Berberina, L., Nikolić, M., Stojanović, S. Đ.,& Zlatović, M.. (2022). Influence of cation−π interactions to the structural stability of phycocyanin proteins: A computational study.. in Computational Biology and Chemistry
Elsevier., 100, 107752.
https://doi.org/10.1016/j.compbiolchem.2022.107752

Berberina L, Nikolić M, Stojanović SĐ, Zlatović M. Influence of cation−π interactions to the structural stability of phycocyanin proteins: A computational study.. in Computational Biology and Chemistry. 2022;100:107752.
doi:10.1016/j.compbiolchem.2022.107752 .

Berberina, Luka, Nikolić, Milan, Stojanović, Srđan Đ., Zlatović, Mario, "Influence of cation−π interactions to the structural stability of phycocyanin proteins: A computational study." in Computational Biology and Chemistry, 100 (2022):107752,
https://doi.org/10.1016/j.compbiolchem.2022.107752 . .