Abstract
Saturation transfer difference (STD) NMR is a technique that provides information on the intermolecular interfaces of heterogenous complexes by cross-saturation from one molecule to the other. In this case, selective saturation of protein protons is applied, and the cross-relaxation to the RNA sample results in a reduction of the peak intensities in the measured H1–H1 NOESY spectrum. This allows for a relatively rapid and simple method of identifying the protein binding interface of an RNA with assigned chemical shift data.
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Acknowledgments
Funding is provided by an NSERC CGS-D scholarship (E.M), Cancer Research Society (Canada) [20085], and Canadian Cancer Society Research Institute [703809].
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McRae, E.K.S., Davidson, D.E., McKenna, S.A. (2020). 2D Saturation Transfer Difference NMR for Determination of Protein Binding Sites on RNA Guanine Quadruplexes. In: Ørom, U. (eds) RNA-Chromatin Interactions. Methods in Molecular Biology, vol 2161. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0680-3_9
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DOI: https://doi.org/10.1007/978-1-0716-0680-3_9
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