Приказ основних података о документу
Aromatic π-networks in Sm/LSm protein interfaces
Aromatična π-mreža u interfejsima Sm/LSm proteina
dc.creator | Breberina, Luka M. | |
dc.creator | Nikolić, Milan | |
dc.creator | Stojanović, Srđan Đ. | |
dc.date.accessioned | 2018-11-22T00:26:33Z | |
dc.date.available | 2018-11-22T00:26:33Z | |
dc.date.issued | 2014 | |
dc.identifier.issn | 0354-4656 | |
dc.identifier.uri | https://cherry.chem.bg.ac.rs/handle/123456789/82 | |
dc.description.abstract | In this work, we have analyzed the influence of π-π interactions on stability and properties of Sm/LSm assemblies. The residues were found to be involved in π-π interactions much more frequently than Tyr or His. Similarly, the Phe-Phe π-π interacting pair had the highest frequency of occurrence. Furthermore, a significant number of π-networks were observed at the interface of Sm/LSm proteins. Generally speaking, the distance between the interacting pairs was in the range of 5-6 Å. 3π and 7π-networks were found to frequently have plane-plane angles less than 60º. Solvent accessibility pattern of Sm/LSm proteins revealed that all of the interacting residues were from buried areas. Moreover, most of the π-π interacting residues of Sm/LSm proteins were evolutionary conserved and were in the strand regions. A high percentage of these residues could be considered as stabilization centers that (significantly) contribute to the net stability of Sm/LSm proteins. | en |
dc.description.abstract | U ovom radu smo analizirali uticaj π-π interakcija na stabilnost i osobine Sm/LSm proteinskih agregata. Ostatak fenilalanina znatno češće uzima učešće u π-π interakcijama u odnosu na His i Tyr. Slično, Phe-Phe π-π interagujući parovi su najučestaliji. Prepoznat je značajan broj π-mreža u interfejsima Sm/LSm proteinima. U većini slučajeva, rastojanje između interagujućih parova aminokiselina bilo je u opsegu 5-6 Å. Za 3π i 7π-mreže, prsten-prsten uglovi manji od 60º su bili učestaliji. Razmatrajući delove Sm/LSm proteina dostupne rastvaraču, može se zaključiti da se svi interagujući parovi nalaze u unutrašnjim regionima. Pored toga, većina π-π interagujućih aminokiselinskih ostataka je evoluciono konzervativan i nalazi se u regionima sa nabranom strukturom. Veliki broj ovih ostataka se može smatrati stabilizacionim centrima, koji (značajno) doprinose ukupnoj stabilnost Sm/LSm proteina. | sr |
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 | openAccess | |
dc.source | Facta Universitatis: Series Physics, Chemistry and Technology | |
dc.subject | aromatic π-networks | en |
dc.subject | Sm/LSm proteins | en |
dc.subject | interfaces | en |
dc.subject | stabilization centers | en |
dc.subject | conservation score | en |
dc.subject | aromatična π-mreža | sr |
dc.subject | Sm/LSm proteini | sr |
dc.subject | interfejs | sr |
dc.subject | stabilizacioni centri | sr |
dc.subject | skor konzervativnosti | sr |
dc.title | Aromatic π-networks in Sm/LSm protein interfaces | en |
dc.title | Aromatična π-mreža u interfejsima Sm/LSm proteina | sr |
dc.type | article | |
dc.rights.license | ARR | |
dc.citation.volume | 12 | |
dc.citation.issue | 1 | |
dc.citation.spage | 27 | |
dc.citation.epage | 39 | |
dc.identifier.doi | 10.2298/FUPCT1401027B | |
dc.citation.other | 12(1): 27-39 | |
dc.citation.rank | M51 | |
dc.type.version | publishedVersion | |
dc.identifier.fulltext | https://cherry.chem.bg.ac.rs/bitstream/id/10012/80.pdf |