Приказ основних података о документу
Contribution of anion-pi interactions to the stability of Sm/LSm proteins
dc.creator | Breberina, Luka M. | |
dc.creator | Milčić, Miloš K. | |
dc.creator | Nikolić, Milan | |
dc.creator | Stojanović, Srđan Đ. | |
dc.date.accessioned | 2018-11-22T00:30:27Z | |
dc.date.available | 2018-11-22T00:30:27Z | |
dc.date.issued | 2015 | |
dc.identifier.issn | 0949-8257 | |
dc.identifier.uri | https://cherry.chem.bg.ac.rs/handle/123456789/1481 | |
dc.description.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. | en |
dc.publisher | Springer, New York | |
dc.relation | info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172001/RS// | |
dc.relation | info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172035/RS// | |
dc.rights | restrictedAccess | |
dc.source | Journal of Biological Inorganic Chemistry | |
dc.subject | Anion-pi interactions | en |
dc.subject | Sm/LSm proteins | en |
dc.subject | Interfaces | en |
dc.subject | Stabilization centers | en |
dc.subject | Interaction energy | en |
dc.title | Contribution of anion-pi interactions to the stability of Sm/LSm proteins | en |
dc.type | article | |
dc.rights.license | ARR | |
dcterms.abstract | Бреберина, Лука М.; Стојановиц, Срдан Д.; Милчић, Милош; Николић, Милан; | |
dc.citation.volume | 20 | |
dc.citation.issue | 3 | |
dc.citation.spage | 475 | |
dc.citation.epage | 485 | |
dc.identifier.wos | 000352212700003 | |
dc.identifier.doi | 10.1007/s00775-014-1227-1 | |
dc.citation.other | 20(3): 475-485 | |
dc.citation.rank | M21 | |
dc.identifier.pmid | 25502146 | |
dc.type.version | publishedVersion | en |
dc.identifier.scopus | 2-s2.0-84928881945 |