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Coupled binding and folding of intrinsically disordered proteins: what can we learn from kinetics?
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Number of Authors: 3
2016 (English)In: Current opinion in structural biology, ISSN 0959-440X, E-ISSN 1879-033X, Vol. 36, 18-24 p.Article in journal (Refereed) Published
Abstract [en]

Protein or protein regions that are not forming well-defined structures in their free states under native-like conditions are called intrinsically disordered proteins. Such proteins are very common in protein-protein interactions, where their disorder apparently gives several advantages including optimal binding properties. To fully appreciate why protein disorder is advantageous for protein-protein interactions we need to understand the mechanism(s) of interaction. However, elucidating mechanisms in protein-protein interactions is usually very challenging. Here we discuss how kinetics in combination with protein engineering and structural information can be used to depict details of protein-protein interactions involving intrinsically disordered proteins.

Place, publisher, year, edition, pages
2016. Vol. 36, 18-24 p.
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-129646DOI: 10.1016/j.sbi.2015.11.012ISI: 000372681200005PubMedID: 26720267OAI: oai:DiVA.org:su-129646DiVA: diva2:924577
Available from: 2016-04-28 Created: 2016-04-26 Last updated: 2016-04-28Bibliographically approved

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Dogan, Jakob
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