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Intrinsically Disordered Proteins Studied by NMR Spectroscopy pp 49–122Cite as

NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and Interactions: General Overview and Practical Guidelines

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 870))

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).

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Authors and Affiliations

  1. CERM and Department of Chemistry “Ugo Schiff”, University of Florence, 50019, Via Luigi Sacconi 6, Sesto Fiorentino, Florence, Italy

    Prof. Isabella C. Felli, Tomáš Hošek, Alessandro Piai & Prof. Roberta Pierattelli

  2. Bruker BioSpin AG, Industriestrasse 26, 8117, Fällanden, Switzerland

    Dr. Sergio Gil-Caballero & Dr. Rainer Kümmerle

  3. Institut de Biologie Structurale, Université Grenoble 1, CNRS, CEA, 71 avenue des Martyrs, 38044, Grenoble Cedex 9, France

    Dr. Bernhard Brutscher & Zsófia Sólyom

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  1. CERM and Department of Chemistry, "Ugo Schiff" University of Florence, Florence, Italy

    Isabella C. Felli

  2. CERM and Department of Chemistry, "Ugo Schiff" University of Florence, Florence, Italy

    Roberta Pierattelli

Appendix

Appendix

Table A.1 High-multidimensional 1H detected experiments for backbone and side-chain resonance assignment
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Table A.2 High-multidimensional 13C detected experiments for backbone and side-chain resonance assignment
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Brutscher, B. et al. (2015). NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and Interactions: General Overview and Practical Guidelines. In: Felli, I., Pierattelli, R. (eds) Intrinsically Disordered Proteins Studied by NMR Spectroscopy. Advances in Experimental Medicine and Biology, vol 870. Springer, Cham. https://doi.org/10.1007/978-3-319-20164-1_3

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