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Intrinsically disordered proteins-relation to general model expressing the active role of the water environment

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Intrinsically disordered proteins-relation to general model expressing the active role of the water environment

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dc.contributor.author Kalinowska, Barbara [USOS61115] pl
dc.contributor.author Banach, Mateusz [SAP20011078] pl
dc.contributor.author Konieczny, Leszek pl
dc.contributor.author Marchewka, Damian [SAP14007465] pl
dc.contributor.author Roterman-Konieczna, Irena [SAP20000474] pl
dc.date.accessioned 2015-06-11T11:01:46Z
dc.date.available 2015-06-11T11:01:46Z
dc.date.issued 2014 pl
dc.identifier.isbn 978-0-12-800168-4 pl
dc.identifier.issn 1876-1623 pl
dc.identifier.uri http://ruj.uj.edu.pl/xmlui/handle/item/9426
dc.language eng pl
dc.rights Dodaję tylko opis bibliograficzny *
dc.rights.uri *
dc.title Intrinsically disordered proteins-relation to general model expressing the active role of the water environment pl
dc.type JournalArticle pl
dc.description.physical 315-346 pl
dc.abstract.en This work discusses the role of unstructured polypeptide chain fragments in shaping the protein's hydrophobic core. Based on the "fuzzy oil drop" model, which assumes an idealized distribution of hydrophobicity density described by the 3D Gaussian, we can determine which fragments make up the core and pinpoint residues whose location conflicts with theoretical predictions. We show that the structural influence of the water environment determines the positions of disordered fragments, leading to the formation of a hydrophobic core overlaid by a hydrophilic mantle. This phenomenon is further described by studying selected proteins which are known to be unstable and contain intrinsically disordered fragments. Their properties are established quantitatively, explaining the causative relation between the protein's structure and function and facilitating further comparative analyses of various structural models. pl
dc.subject.en fuzzy oil drop model pl
dc.subject.en hydrophobicity pl
dc.subject.en intrinsically disordered proteins pl
dc.description.volume 94 pl
dc.description.publication 2 pl
dc.identifier.doi 10.1016/B978-0-12-800168-4.00008-1 pl
dc.identifier.eissn 1876-1631 pl
dc.title.journal Advances in Protein Chemistry and Structural Biology pl
dc.language.container eng pl
dc.affiliation Wydział Fizyki, Astronomii i Informatyki Stosowanej pl
dc.affiliation Wydział Lekarski : Zakład Bioinformatyki i Telemedycyny pl
dc.subtype Article pl
dc.rights.original bez licencji pl
dc.cm.id 64979
.pointsMNiSW [2014 A]: 30


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