Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 36, Issue -, Pages 18-24Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2015.11.012
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Funding
- Swedish Research Council [2012-5096, 2014-4299]
- Italian Ministero dell 'Istruzione dell'Universita' e della Ricerca (Progetto di Interesse 'Invecchiamento')
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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.
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