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.
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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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