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Coupled binding and folding of intrinsically disordered proteins: what can we learn from kinetics?
Univ Roma La Sapienza, Ist Pasteur, Fdn Cenci Bolognetti, Piazzale Aldo Moro 5, I-00185 Rome, Italy.;Univ Roma La Sapienza, Ist Biol & Patol Mol, CNR, Dipartimento Sci Biochim A Rossi Fanelli, Piazzale Aldo Moro 5, I-00185 Rome, Italy.;Univ Cambridge, Dept Chem, Lensfield Rd, Cambridge CB2 1EW, England..
Stockholm Univ, Dept Biochem & Biophys, SE-10691 Stockholm, Sweden..
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
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
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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
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
URN: urn:nbn:se:uu:diva-294591DOI: 10.1016/j.sbi.2015.11.012ISI: 000372681200005PubMedID: 26720267OAI: oai:DiVA.org:uu-294591DiVA: diva2:931005
Funder
Swedish Research Council, 2012-5096, 2014-4299
Available from: 2016-05-26 Created: 2016-05-25 Last updated: 2016-05-26Bibliographically approved

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