Alanine scanning effects on the biochemical and viophysical properties of intrinsically disordered proteins: a case study of the histidine to alanine mutations in amyloid-beta(42)

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dc.contributor.authorWeber, Orkide Coşkuner
dc.contributor.authorUversky, Vladimir N.
dc.date.accessioned2021-01-08T21:51:23Z
dc.date.available2021-01-08T21:51:23Z
dc.date.issued2019
dc.departmentTAÜ, Fen Fakültesi, Moleküler Biyoteknoloji Bölümüen_US
dc.descriptionUversky, Vladimir N./0000-0002-4037-5857; Coskuner, Orkid/0000-0002-0772-9350en_US
dc.descriptionWOS:000459948700023en_US
dc.descriptionPubMed: 30694660en_US
dc.description.abstractAlanine scanning is a tool in molecular biology that is commonly used to evaluate the contribution of a specific amino acid residue to the stability and function of a protein. Additionally, this tool is also used to understand whether the side chain of a specific amino acid residue plays a role in the protein's bioactivity. Furthermore, computational alanine scanning methods are utilized to predict the thermodynamic properties of proteins. These studies are utilized with the assumption that the biochemical and biophysical properties of a protein do not change with alanine scanning. Our study was dedicated to analyze the effect of alanine scanning on the biochemical and biophysical properties of intrinsically disordered proteins. To this end, we studied the impact of widely used histidine to alanine mutations in amyloid-beta (A beta). We found that the secondary and tertiary contacts, salt bridge formations, and thermodynamic properties, as well as disorder propensities and aggregation predisposition of A beta, are impacted by the single and triple point histidine to alanine mutations. Experimental and computational studies employing the alanine scanning technique for mutating histidine to alanine in the analysis of intrinsically disordered proteins have to consider these effects.
dc.identifier.doi10.1021/acs.jcim.8b00926
dc.identifier.endpage884en_US
dc.identifier.issn1549-9596
dc.identifier.issn1549-960X
dc.identifier.issue2en_US
dc.identifier.scopus2-s2.0-85061554663
dc.identifier.scopusqualityQ1
dc.identifier.startpage871en_US
dc.identifier.urihttp://doi.org/10.1021/acs.jcim.8b00926
dc.identifier.urihttps://hdl.handle.net/20.500.12846/199
dc.identifier.volume59en_US
dc.identifier.wosWOS:000459948700023
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.institutionauthorWeber, Orkide Coşkuner
dc.language.isoen
dc.publisherAmer Chemical Soc
dc.relation.ispartofJournal Of Chemical Information And Modeling
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.titleAlanine scanning effects on the biochemical and viophysical properties of intrinsically disordered proteins: a case study of the histidine to alanine mutations in amyloid-beta(42)
dc.typeArticle

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