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dc.creatorStanković, Ivana
dc.creatorNiu, Shuqiang
dc.creatorHall, Michael B.
dc.creatorZarić, Snežana D.
dc.date.accessioned2020-08-07T10:47:57Z
dc.date.available2020-08-07T10:47:57Z
dc.date.issued2020
dc.identifier.issn0141-8130
dc.identifier.urihttp://cer.ihtm.bg.ac.rs/handle/123456789/3606
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.en
dc.language.isoensr
dc.publisherElseviersr
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172065/RS//sr
dc.relationNPRP grant from the Qatar National Research Fund (a member of the Qatar Foundation) [grant number NPRP8-425-1-087].sr
dc.relationNSF (CHE-1664866)sr
dc.rightsrestrictedAccesssr
dc.sourceInternational Journal of Biological Macromoleculessr
dc.subjectAmyloidssr
dc.subjectAromatic amino acidssr
dc.subjectSelf-assemblysr
dc.titleRole of aromatic amino acids in amyloid self-assemblyen
dc.typearticlesr
dc.rights.licenseARRsr
dcterms.abstractНиу, Схуqианг; Халл, Мицхаел Б.; Зарић, Снежана Д.; Станковић, Ивана М.;
dc.citation.volume156
dc.citation.spage949
dc.citation.epage959
dc.citation.rankaM21~
dc.description.otherThe peer-reviewed version: [http://cer.ihtm.bg.ac.rs/handle/123456789/3609]
dc.identifier.pmid32199918
dc.identifier.doi10.1016/j.ijbiomac.2020.03.064
dc.identifier.scopus2-s2.0-85085469915
dc.identifier.wos000538104200097
dc.type.versionpublishedVersionsr


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