title: NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and Interactions: General Overview and Practical Guidelines.
abstract: Thanks to recent improvements in NMR instrumentation, pulse sequence design, and sample preparation, a panoply of new NMR tools has become available for atomic resolution characterization of intrinsically disordered proteins (IDPs) that are optimized for the particular chemical and spectroscopic properties of these molecules. A wide range of NMR observables can now be measured on increasingly complex IDPs that report on their structural and dynamic properties in isolation, as part of a larger complex, or even inside an entire living cell. Herein we present basic NMR concepts, as well as optimised tools available for the study of IDPs in solution. In particular, the following sections are discussed hereafter: a short introduction to NMR spectroscopy and instrumentation (Sect. 3.1), the effect of order and disorder on NMR observables (Sect. 3.2), particular challenges and bottlenecks for NMR studies of IDPs (Sect. 3.3), 2D HN and CON NMR experiments: the fingerprint of an IDP (Sect. 3.4), tools for overcoming major bottlenecks of IDP NMR studies (Sect. 3.5), 13C detected experiments (Sect. 3.6), from 2D to 3D: from simple snapshots to site-resolved characterization of IDPs (Sect. 3.7), sequential NMR assignment: 3D experiments (Sect. 3.8), high-dimensional NMR experiments (nD, with n>3) (Sect. 3.9) and conclusions and perspectives (Sect. 3.10).
authors.affiliation: Institut de Biologie Structurale, Université Grenoble 1, CNRS, CEA, 71 avenue des Martyrs, 38044, Grenoble Cedex 9, France. bernhard.brutscher@ibs.fr.
authors.forename: Bernhard
authors.initials: B
authors.lastname: Brutscher
authors.affiliation: CERM and Department of Chemistry "Ugo Schiff", University of Florence, 50019, Via Luigi Sacconi 6, Sesto Fiorentino, Florence, Italy. felli@cerm.unifi.it.
authors.forename: Isabella C
authors.initials: IC
authors.lastname: Felli
authors.affiliation: Bruker BioSpin AG, Industriestrasse 26, 8117, Fällanden, Switzerland.
authors.forename: Sergio
authors.initials: S
authors.lastname: Gil-Caballero
authors.affiliation: CERM and Department of Chemistry "Ugo Schiff", University of Florence, 50019, Via Luigi Sacconi 6, Sesto Fiorentino, Florence, Italy.
authors.forename: Tomáš
authors.initials: T
authors.lastname: Hošek
authors.affiliation: Bruker BioSpin AG, Industriestrasse 26, 8117, Fällanden, Switzerland.
authors.forename: Rainer
authors.initials: R
authors.lastname: Kümmerle
authors.affiliation: CERM and Department of Chemistry "Ugo Schiff", University of Florence, 50019, Via Luigi Sacconi 6, Sesto Fiorentino, Florence, Italy.
authors.forename: Alessandro
authors.initials: A
authors.lastname: Piai
authors.affiliation: CERM and Department of Chemistry "Ugo Schiff", University of Florence, 50019, Via Luigi Sacconi 6, Sesto Fiorentino, Florence, Italy. pierattelli@cerm.unifi.it.
authors.forename: Roberta
authors.initials: R
authors.lastname: Pierattelli
authors.affiliation: Institut de Biologie Structurale, Université Grenoble 1, CNRS, CEA, 71 avenue des Martyrs, 38044, Grenoble Cedex 9, France.
authors.forename: Zsófia
authors.initials: Z
authors.lastname: Sólyom
mesh_terms: D064267:Intrinsically Disordered Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation
chemical_list: D064267:Intrinsically Disordered Proteins
keywords: 13C detection; BEST; NMR basics; NMR instrumentation; Sequential assignment; high dimensional NMR; pulse sequences