title: Structure and Dynamics of Intrinsically Disordered Proteins.
abstract: Intrinsically disordered proteins (IDPs) are involved in a wide range of essential biological processes, including in particular signalling and regulation. We are only beginning, however, to develop a detailed knowledge of the structure and dynamics of these proteins. It is becoming increasingly clear that, as IDPs populate highly heterogeneous states, they should be described in terms of conformational ensembles rather than as individual structures, as is instead most often the case for the native states of globular proteins. Within this context, in this chapter we describe the conceptual tools and methodological aspects associated with the description of the structure and dynamics of IDPs in terms of conformational ensembles. A major emphasis is given to methods in which molecular simulations are used in combination with experimental nuclear magnetic resonance (NMR) measurements, as they are emerging as a powerful route to achieve an accurate determination of the conformational properties of IDPs.
authors.affiliation: Department of Chemistry, University of Cambridge, CB2 1EW, Cambridge, UK.
authors.forename: Biao
authors.initials: B
authors.lastname: Fu
authors.affiliation: Department of Chemistry, University of Cambridge, CB2 1EW, Cambridge, UK. mv245@cam.ac.uk.
authors.forename: Michele
authors.initials: M
authors.lastname: Vendruscolo
mesh_terms: D064267:Intrinsically Disordered Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation
chemical_list: D064267:Intrinsically Disordered Proteins
keywords: Conformational ensembles; Dynamics; Molecular dynamics; Structure