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Characterizing Protein-Protein Interactions Using Solution NMR Spectroscopy

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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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
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: Faculties > Sciences > School of Biosciences
Depositing User: Jose Ortega-Roldan
Date Deposited: 02 Nov 2018 17:09 UTC
Last Modified: 09 Aug 2019 09:12 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/69896 (The current URI for this page, for reference purposes)
Ortega-Roldan, Jose L.: https://orcid.org/0000-0002-6316-4390
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