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. 2023:2651:69-83.
doi: 10.1007/978-1-0716-3084-6_5.

NMR Titration Studies in Z-DNA Dynamics

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NMR Titration Studies in Z-DNA Dynamics

Seo-Ree Choi et al. Methods Mol Biol. 2023.

Abstract

Chemical shift perturbation (CSP) is a simple NMR technique for studying the DNA binding of proteins. Titration of the unlabeled DNA into the 15N-labeled protein is monitored by acquiring a two-dimensional (2D) heteronuclear single-quantum correlation (HSQC) spectrum at each step of the titration. CSP can also provide information on the DNA-binding dynamics of proteins, as well as protein-induced conformational changes in DNA. Here, we describe the titration of DNA for the 15N-labeled Z-DNA-binding protein, monitored via 2D HSQC spectra. NMR titration data can be analyzed with the active B-Z transition model to provide the protein-induced B-Z transition dynamics of DNA.

Keywords: Chemical shift perturbation; DNA–protein interaction; Dynamics; NMR; Titration; Z-DNA; Z-DNA-binding protein.

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References

    1. Williamson MP (2013) Using chemical shift perturbation to characterise ligand binding. Prog Nucl Mag Res Sp 73:1–16 - DOI
    1. Zuiderweg ER (2002) Mapping protein-protein interactions in solution by NMR spectroscopy. Biochemistry 41:1–7 - DOI - PubMed
    1. McCoy MA, Wyss DF (2002) Spatial localization of ligand binding sites from electron current density surfaces calculated from NMR chemical shift perturbations. J Am Chem Soc 124:11758–11763 - DOI - PubMed
    1. Fielding L (2007) NMR methods for the determination of protein–ligand dissociation constants. Prog NMR Spectrosc 51:219–242 - DOI
    1. Arai M, Ferreon JC, Wright PE (2012) Quantitative analysis of multisite protein-ligand interactions by NMR: binding of intrinsically disordered p53 transactivation subdomains with the TAZ2 domain of CBP. J Am Chem Soc 134:3792–3803 - DOI - PubMed - PMC

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