title: From sequence and forces to structure, function, and evolution of intrinsically disordered proteins.
abstract: Intrinsically disordered proteins (IDPs), which lack persistent structure, are a challenge to structural biology due to the inapplicability of standard methods for characterization of folded proteins as well as their deviation from the dominant structure/function paradigm. Their widespread presence and involvement in biological function, however, has spurred the growing acceptance of the importance of IDPs and the development of new tools for studying their structure, dynamics, and function. The interplay of folded and disordered domains or regions for function and the existence of a continuum of protein states with respect to conformational energetics, motional timescales, and compactness are shaping a unified understanding of structure-dynamics-disorder/function relationships. In the 20(th) anniversary of Structure, we provide a historical perspective on the investigation of IDPs and summarize the sequence features and physical forces that underlie their unique structural, functional, and evolutionary properties.
authors.affiliation: Molecular Structure and Function, Hospital for Sick Children, Toronto, ON, M5G 1X8, Canada; Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada. Electronic address: forman@sickkids.ca.
authors.forename: Julie D
authors.initials: JD
authors.lastname: Forman-Kay
authors.forename: Tanja
authors.initials: T
authors.lastname: Mittag
mesh_terms: D000595:Amino Acid Sequence; D019277:Entropy; D019143:Evolution, Molecular; D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D064267:Intrinsically Disordered Proteins