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Please use this identifier to cite or link to this item: https://research.matf.bg.ac.rs/handle/123456789/341
DC FieldValueLanguage
dc.contributor.authorNinković, Dragan Ben_US
dc.contributor.authorAndrić, Jelena Men_US
dc.contributor.authorMalkov, Sašaen_US
dc.contributor.authorZarić, Snežana Den_US
dc.date.accessioned2022-08-10T12:10:00Z-
dc.date.available2022-08-10T12:10:00Z-
dc.date.issued2014-
dc.identifier.issn14639076en
dc.identifier.urihttps://research.matf.bg.ac.rs/handle/123456789/341-
dc.description.abstractThe data from protein structures from the Protein Data Bank and quantum chemical calculations indicate the importance of aromatic-aromatic interactions at large horizontal displacements (offsets). The protein stacking interactions of the phenylalanine residue show preference for large offsets (3.5-5.0 Å), while the calculations show substantially strong interactions, of about -2.0 kcal mol(-1).en
dc.language.isoenen
dc.relation.ispartofPhysical chemistry chemical physics : PCCPen_US
dc.subject.meshBenzeneen
dc.subject.meshProteinsen
dc.subject.meshQuantum Theoryen
dc.titleWhat are the preferred horizontal displacements of aromatic-aromatic interactions in proteins? Comparison with the calculated benzene-benzene potential energy surfaceen_US
dc.typeArticleen_US
dc.identifier.doi10.1039/c3cp54474e-
dc.identifier.pmid24805772-
dc.identifier.scopus2-s2.0-84901267472-
dc.identifier.urlhttps://api.elsevier.com/content/abstract/scopus_id/84901267472-
dc.contributor.affiliationInformatics and Computer Scienceen_US
dc.relation.firstpage11173en_US
dc.relation.lastpage11177en_US
dc.relation.volume16en_US
dc.relation.issue23en_US
item.fulltextNo Fulltext-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.openairetypeArticle-
crisitem.author.deptInformatics and Computer Science-
crisitem.author.orcid0000-0002-4385-6322-
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