Contribution of anion-pi interactions to the stability of Sm/LSm proteins
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2015
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We have analyzed the influence of anion-pi interactions to the stability of Sm/LSm assemblies. The side chain of Glu is more likely to be in anion-pi interactions than Asp. Phe has the highest occurrence in these interactions than the other two pi residues. Among the anion-pi residue pairs, Glu-Phe residue pair showed the maximum number of anion-pi. We have found hot-spot residues forming anion-pi interactions, and Glu-Phe is the most common hot-spot interacting pair. The significant numbers of anion-pi interacting residues identified in the dataset were involved in the formation of multiple anion-pi interactions. More than half of the residues involved in these interactions are evolutionarily conserved. The anion-pi interaction energies are distance and orientation dependent. It was found that anion-pi interactions showed energy less than -15 kcal mol(-1), and most of them have energy in the range -2 to -9 kcal mol(-1). Solvent accessibility pattern of Sm/LSm proteins reveals that all... of the interacting residues are preferred to be in buried regions. Most of the interacting residues preferred to be in strand. A significant percentage of anion-pi interacting residues are located as stabilization centers and thus might provide additional stability to these proteins. The simultaneous interaction of anions and cations on different faces of the same pi-system has been observed. On the whole, the results presented in this work will be very useful for understanding the contribution of anion-pi interaction to the stability of Sm/LSm proteins.
Ključne reči:
Anion-pi interactions / Sm/LSm proteins / Interfaces / Stabilization centers / Interaction energyIzvor:
Journal of Biological Inorganic Chemistry, 2015, 20, 3, 475-485Izdavač:
- Springer, New York
Finansiranje / projekti:
- Proučavanje fizičkohemijskih i biohemijskih procesa u životnoj sredini koji utiču na zagađenje i istraživanje mogućnosti za minimiziranje posledica (RS-MESTD-Basic Research (BR or ON)-172001)
- Racionalni dizajn i sinteza biološki aktivnih i koordinacionih jedinjenja i funkcionalnih materijala, relevantnih u (bio)nanotehnologiji (RS-MESTD-Basic Research (BR or ON)-172035)
DOI: 10.1007/s00775-014-1227-1
ISSN: 0949-8257
PubMed: 25502146
WoS: 000352212700003
Scopus: 2-s2.0-84928881945
Institucija/grupa
IHTMTY - JOUR AU - Breberina, Luka M. AU - Milčić, Miloš AU - Nikolić, Milan AU - Stojanović, Srđan PY - 2015 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/1693 AB - We have analyzed the influence of anion-pi interactions to the stability of Sm/LSm assemblies. The side chain of Glu is more likely to be in anion-pi interactions than Asp. Phe has the highest occurrence in these interactions than the other two pi residues. Among the anion-pi residue pairs, Glu-Phe residue pair showed the maximum number of anion-pi. We have found hot-spot residues forming anion-pi interactions, and Glu-Phe is the most common hot-spot interacting pair. The significant numbers of anion-pi interacting residues identified in the dataset were involved in the formation of multiple anion-pi interactions. More than half of the residues involved in these interactions are evolutionarily conserved. The anion-pi interaction energies are distance and orientation dependent. It was found that anion-pi interactions showed energy less than -15 kcal mol(-1), and most of them have energy in the range -2 to -9 kcal mol(-1). Solvent accessibility pattern of Sm/LSm proteins reveals that all of the interacting residues are preferred to be in buried regions. Most of the interacting residues preferred to be in strand. A significant percentage of anion-pi interacting residues are located as stabilization centers and thus might provide additional stability to these proteins. The simultaneous interaction of anions and cations on different faces of the same pi-system has been observed. On the whole, the results presented in this work will be very useful for understanding the contribution of anion-pi interaction to the stability of Sm/LSm proteins. PB - Springer, New York T2 - Journal of Biological Inorganic Chemistry T1 - Contribution of anion-pi interactions to the stability of Sm/LSm proteins VL - 20 IS - 3 SP - 475 EP - 485 DO - 10.1007/s00775-014-1227-1 ER -
@article{ author = "Breberina, Luka M. and Milčić, Miloš and Nikolić, Milan and Stojanović, Srđan", year = "2015", abstract = "We have analyzed the influence of anion-pi interactions to the stability of Sm/LSm assemblies. The side chain of Glu is more likely to be in anion-pi interactions than Asp. Phe has the highest occurrence in these interactions than the other two pi residues. Among the anion-pi residue pairs, Glu-Phe residue pair showed the maximum number of anion-pi. We have found hot-spot residues forming anion-pi interactions, and Glu-Phe is the most common hot-spot interacting pair. The significant numbers of anion-pi interacting residues identified in the dataset were involved in the formation of multiple anion-pi interactions. More than half of the residues involved in these interactions are evolutionarily conserved. The anion-pi interaction energies are distance and orientation dependent. It was found that anion-pi interactions showed energy less than -15 kcal mol(-1), and most of them have energy in the range -2 to -9 kcal mol(-1). Solvent accessibility pattern of Sm/LSm proteins reveals that all of the interacting residues are preferred to be in buried regions. Most of the interacting residues preferred to be in strand. A significant percentage of anion-pi interacting residues are located as stabilization centers and thus might provide additional stability to these proteins. The simultaneous interaction of anions and cations on different faces of the same pi-system has been observed. On the whole, the results presented in this work will be very useful for understanding the contribution of anion-pi interaction to the stability of Sm/LSm proteins.", publisher = "Springer, New York", journal = "Journal of Biological Inorganic Chemistry", title = "Contribution of anion-pi interactions to the stability of Sm/LSm proteins", volume = "20", number = "3", pages = "475-485", doi = "10.1007/s00775-014-1227-1" }
Breberina, L. M., Milčić, M., Nikolić, M.,& Stojanović, S.. (2015). Contribution of anion-pi interactions to the stability of Sm/LSm proteins. in Journal of Biological Inorganic Chemistry Springer, New York., 20(3), 475-485. https://doi.org/10.1007/s00775-014-1227-1
Breberina LM, Milčić M, Nikolić M, Stojanović S. Contribution of anion-pi interactions to the stability of Sm/LSm proteins. in Journal of Biological Inorganic Chemistry. 2015;20(3):475-485. doi:10.1007/s00775-014-1227-1 .
Breberina, Luka M., Milčić, Miloš, Nikolić, Milan, Stojanović, Srđan, "Contribution of anion-pi interactions to the stability of Sm/LSm proteins" in Journal of Biological Inorganic Chemistry, 20, no. 3 (2015):475-485, https://doi.org/10.1007/s00775-014-1227-1 . .