Приказ основних података о документу

dc.creatorZarić, Božidarka L.
dc.creatorJovanović, Vesna B.
dc.creatorStojanović, Srđan Đ.
dc.date.accessioned2018-11-22T00:17:55Z
dc.date.available2018-11-22T00:17:55Z
dc.date.issued2011
dc.identifier.issn0022-5193
dc.identifier.urihttps://cherry.chem.bg.ac.rs/handle/123456789/1140
dc.description.abstractThe distinguishing property of Sm protein associations is their high stability. In order to understand this property, we analyzed the interface non-covalent interactions and compared the properties of the Sm protein interfaces with those of a test set, Binding Interface Database (BID). The comparison revealed that the main differences between interfaces of Sm proteins and those of the BID set are the content of charged residues, hydrogen bonds, salt bridges, and conservation scores of interface residues. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surface, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Both interfaces of Sm proteins and of test set have a similar number of hydrophobic interactions per 100 angstrom(2). The interfaces of Sm proteins have substantially more hydrogen bonds than the interfaces in test set. The results show clearly that the interfaces of Sm proteins form more salt bridges compared with test set. On average, there are about 16 salt bridges per interface. The high conservation score of amino acids that are involved in non-covalent interactions in protein interfaces is an additional strong argument for their importance. The overriding conclusion from this study is that the non-covalent interactions in Sm protein interfaces considerably contribute to stability of higher order structures. (C) 2010 Elsevier Ltd. All rights reserved.en
dc.publisherAcademic Press Ltd- Elsevier Science Ltd, London
dc.relationinfo:eu-repo/grantAgreement/MESTD/MPN2006-2010/142037/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/MPN2006-2010/142020/RS//
dc.rightsrestrictedAccess
dc.sourceJournal of Theoretical Biology
dc.subjectInterfaceen
dc.subjectSm proteinsen
dc.subjectHydrogen bondsen
dc.subjectHydrophobic interactionsen
dc.subjectSalt bridgesen
dc.titleNon-covalent interactions across subunit interfaces in Sm proteinsen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractЗариц, Бозидарка Л.; Стојановиц, Срдан Д.; Јовановић, Весна;
dc.citation.volume271
dc.citation.issue1
dc.citation.spage18
dc.citation.epage26
dc.identifier.wos000286492100003
dc.identifier.doi10.1016/j.jtbi.2010.11.025
dc.citation.other271(1): 18-26
dc.citation.rankM21
dc.identifier.pmid21095194
dc.type.versionpublishedVersionen
dc.identifier.scopus2-s2.0-78649761217


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Приказ основних података о документу