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dc.creatorRibić, Vesna
dc.creatorStojanović, Srđan
dc.creatorZlatović, Mario
dc.date.accessioned2019-10-14T11:56:25Z
dc.date.available2018-08-07
dc.date.available2019-10-14T11:56:25Z
dc.date.issued2018
dc.identifier.issn0141-8130
dc.identifier.urihttp://cherry.chem.bg.ac.rs/handle/123456789/3151
dc.identifier.urihttps://cer.ihtm.bg.ac.rs/handle/123456789/3140
dc.description.abstractWe investigated 1060 possible anion-pi interactions in a data set of 41 superoxide dismutase active centers. Our observations indicate that majority of the aromatic residues are capable to form anion-pi interactions, mainly by long-range contacts, and that there is preference of Trp over other aromatic residues in these interactions. Furthermore, 68% of total predicted interactions in the dataset are multiple anion-pi interactions. Anion-pi interactions are distance and orientation dependent. We analyzed the energy contribution resulting from anion-pi interactions using ab initio calculations. The results showed that, while most of their interaction energies lay in the range from -0 to -4 kcal mol(-1), those energies can be up to -9 kcal mol(-1) and about 34% of interactions were found to be repulsive. Majority of the suggested anion-pi interacting residues in ternary complexes are metal-assisted. Stabilization centers for these proteins showed that all the six residues found in predicted anion-pi interactions are important in locating one or more of such centers. The anion-pi interacting residues in these proteins were found to be highly conserved. We hope that these studies might contribute useful information regarding structural stability and its interaction in future designs of novel metalloproteins. (C) 2017 Elsevier B.V. All rights reserved.en
dc.publisherElsevier
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172001/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172055/RS//
dc.rightsembargoedAccess
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.sourceInternational Journal of Biological Macromolecules
dc.subjectAnion-pi interactionsen
dc.subjectSuperoxide dismutaseen
dc.subjectProteinsen
dc.subjectActive centersen
dc.subjectInteraction energyen
dc.titleAnion-pi interactions in active centers of superoxide dismutasesen
dc.typearticle
dc.rights.licenseBY-NC-ND
dcterms.abstractРибић, Весна Р.; Златовић, Марио; Стојановић, Срђан Ђ.;
dc.citation.volume106
dc.citation.spage559
dc.citation.epage568
dc.citation.other106: 559-568
dc.citation.rankaM21
dc.description.otherThis is peer-reviewed version of the following article: Ribić, V. R.; Stojanović, S. Đ.; Zlatović, M. V. Anion–π Interactions in Active Centers of Superoxide Dismutases. International Journal of Biological Macromolecules 2018, 106, 559–568. [https://doi.org/10.1016/j.ijbiomac.2017.08.050]
dc.description.otherPublished version: [http://cer.ihtm.bg.ac.rs/handle/123456789/2457]
dc.identifier.pmid28811207
dc.identifier.doi10.1016/j.ijbiomac.2017.08.050
dc.identifier.fulltexthttps://cer.ihtm.bg.ac.rs/bitstream/id/14184/Anion-pi_interactions_acc_2018.pdf
dc.identifier.scopus2-s2.0-85028012582
dc.identifier.wos000417661600063
dc.type.versionacceptedVersionen


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