Ortega-Roldan, Jose L. and Blackledge, Martin and Ringkjøbing Jensen, Malene (2018) Characterizing Protein-Protein Interactions Using Solution NMR Spectroscopy. In: Marsh, Joseph A., ed. Protein Complex Assembly: Methods and Protocols. Methods in Molecular Biology . Humana Press. ISBN 978-1-4939-7758-1. (doi:10.1007/978-1-4939-7759-8_5) (Access to this publication is currently restricted. You may be able to access a copy if URLs are provided) (KAR id:69896)
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Official URL: https://doi.org/10.1007/978-1-4939-7759-8_5 |
Abstract
In this chapter, we describe how NMR chemical shift titrations can be used to study the interaction between two proteins with emphasis on mapping the interface of the complex and determining the bind- ing affinity from a quantitative analysis of the experimental data. In particular, we discuss the appearance of NMR spectra in different chemical exchange regimes (fast, intermediate, and slow) and how these regimes affect NMR data analysis.
Item Type: | Book section |
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DOI/Identification number: | 10.1007/978-1-4939-7759-8_5 |
Uncontrolled keywords: | Protein-protein interactions, Solution NMR spectroscopy, Binding affinity, Dissociation constant, Chemical shift titration, Chemical exchange |
Subjects: |
Q Science Q Science > Q Science (General) Q Science > QR Microbiology |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | Jose Ortega Roldan |
Date Deposited: | 02 Nov 2018 17:09 UTC |
Last Modified: | 05 Nov 2024 12:32 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/69896 (The current URI for this page, for reference purposes) |
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