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NMR Lineshape Analysis of Intrinsically Disordered Protein Interactions

Waudby, CA; Christodoulou, J; (2020) NMR Lineshape Analysis of Intrinsically Disordered Protein Interactions. Intrinsically Disordered Proteins , 2141 pp. 477-504. 10.1007/978-1-0716-0524-0_24. Green open access

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Abstract

Interactions of intrinsically disordered proteins are central to their cellular functions, and solution-state NMR spectroscopy provides a powerful tool for characterizing both structural and mechanistic aspects of such interactions. Here we focus on the analysis of IDP interactions using NMR titration measurements. Changes in resonance lineshapes in two-dimensional NMR spectra upon titration with a ligand contain rich information on structural changes in the protein and the thermodynamics and kinetics of the interaction, as well as on the microscopic association mechanism. Here we present protocols for the optimal design of titration experiments, data acquisition, and data analysis by two-dimensional lineshape fitting using the TITAN software package.

Type: Article
Title: NMR Lineshape Analysis of Intrinsically Disordered Protein Interactions
Location: United States
Open access status: An open access version is available from UCL Discovery
DOI: 10.1007/978-1-0716-0524-0_24
Publisher version: https://doi.org/10.1007/978-1-0716-0524-0_24
Language: English
Additional information: © The Author(s) 2020. This chapter is licensed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/).
Keywords: Binding, IDP, Kinetics, Nuclear magnetic resonance, Titrations
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: https://discovery.ucl.ac.uk/id/eprint/10106394
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