title: Coupled binding and folding of intrinsically disordered proteins: what can we learn from kinetics?
abstract: 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.
authors.affiliation: Istituto Pasteur - Fondazione Cenci Bolognetti and Istituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Scienze Biochimiche "A. Rossi Fanelli" Sapienza, University of Rome, Rome 00185, Italy; Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
authors.forename: Stefano
authors.initials: S
authors.lastname: Gianni
authors.affiliation: Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
authors.forename: Jakob
authors.initials: J
authors.lastname: Dogan
authors.affiliation: Department of Medical Biochemistry and Microbiology, Uppsala University, BMC Box 582, SE-75123 Uppsala, Sweden. Electronic address: Per.Jemth@imbim.uu.se.
authors.forename: Per
authors.initials: P
authors.lastname: Jemth
mesh_terms: D000818:Animals; D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D064267:Intrinsically Disordered Proteins