Приказ основних података о документу

dc.creatorStanković, Ivana M.
dc.creatorNiu, Shuqiang
dc.creatorHall, Michael B.
dc.creatorZarić, Snežana D.
dc.date.accessioned2020-10-14T07:41:37Z
dc.date.available2020-10-14T07:41:37Z
dc.date.issued2020
dc.identifier.issn0141-8130
dc.identifier.issn1879-0003
dc.identifier.urihttps://cherry.chem.bg.ac.rs/handle/123456789/4176
dc.description.abstractAmyloids are proteins of a cross-β structure found as deposits in several diseases and also in normal tissues (nails, spider net, silk). Aromatic amino acids are frequently found in amyloid deposits. Although they are not indispensable, aromatic amino acids, phenylalanine, tyrosine and tryptophan, enhance significantly the kinetics of formation and thermodynamic stability, while tape or ribbon-like morphology is represented in systems with experimentally detected π-π interactions between aromatic rings. Analysis of geometries and energies of the amyloid PDB structures indicate the prevalence of aromatic-nonaromatic interactions and confirm that aromatic-aromatic interactions are not crucial for the amyloid formation.
dc.publisherElsevier
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172065/RS//
dc.relationNPRP grant from the Qatar National Research Fund (a member of the Qatar Foundation) [grant number NPRP8-425-1-087 ]
dc.relationSupport from the NSF ( CHE-1664866 )
dc.rightsrestrictedAccess
dc.sourceInternational Journal of Biological Macromolecules
dc.subjectAmyloids
dc.subjectAromatic amino acids
dc.subjectSelf-assembly
dc.titleRole of aromatic amino acids in amyloid self-assembly
dc.typearticle
dc.rights.licenseARR
dcterms.abstractСтанковић, Ивана М.; Зарић, Снежана Д.; Халл, Мицхаел Б.; Ниу, Схуqианг;
dc.citation.volume156
dc.citation.spage949
dc.citation.epage959
dc.identifier.wos000538104200097
dc.identifier.doi10.1016/j.ijbiomac.2020.03.064
dc.citation.rankaM21
dc.type.versionpublishedVersion
dc.identifier.scopus2-s2.0-85085469915


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Приказ основних података о документу