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Aromatična π-mreža u interfejsima Sm/LSm proteina

dc.creatorBreberina, Luka M.
dc.creatorNikolić, Milan
dc.creatorStojanović, Srđan
dc.date.accessioned2019-01-30T17:40:14Z
dc.date.available2019-01-30T17:40:14Z
dc.date.issued2014
dc.identifier.issn0354-4656
dc.identifier.urihttp://cer.ihtm.bg.ac.rs/handle/123456789/1468
dc.description.abstractIn 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.abstractU 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.publisherUniverzitet u Nišu
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172001/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172035/RS//
dc.rightsopenAccess
dc.sourceFacta universitatis - series: Physics, Chemistry and Technology
dc.subjectaromatic π-networksen
dc.subjectSm/LSm proteinsen
dc.subjectinterfacesen
dc.subjectstabilization centersen
dc.subjectconservation scoreen
dc.subjectaromatična π-mrežasr
dc.subjectSm/LSm proteinisr
dc.subjectinterfejssr
dc.subjectstabilizacioni centrisr
dc.subjectskor konzervativnostisr
dc.titleAromatic π-networks in Sm/LSm protein interfacesen
dc.titleAromatična π-mreža u interfejsima Sm/LSm proteinasr
dc.typearticle
dc.rights.licenseARR
dcterms.abstractСтојановић, Срђан; Николић, Милан Р.; Бреберина, Лука М.; Aроматична π-мрежа у интерфејсима См/ЛСм протеина; Aроматична π-мрежа у интерфејсима См/ЛСм протеина;
dc.citation.volume12
dc.citation.issue1
dc.citation.spage27
dc.citation.epage39
dc.citation.other12(1): 27-39
dc.citation.rankM51
dc.identifier.doi10.2298/FUPCT1401027B
dc.identifier.rcubConv_351
dc.identifier.fulltexthttp://cer.ihtm.bg.ac.rs//bitstream/id/7941/1466.pdf
dc.type.versionpublishedVersion


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