@inbook{a05977a5d21a49eb9812464a3a3f6880,
title = "2D saturation transfer difference nmr for determination of protein binding sites on rna guanine quadruplexes",
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.",
keywords = "NMR, Quadruplex, RNA–protein interactions, Saturation transfer difference, TERRA",
author = "McRae, {Ewan K.S.} and Davidson, {David E.} and McKenna, {Sean A.}",
note = "Funding Information: is provided by an NSERC CGS-D scholarship (E.M), Cancer Research Society (Canada) [20085], and Canadian Cancer Society Research Institute [703809]. Publisher Copyright: {\textcopyright} Springer Science+Business Media, LLC, part of Springer Nature 2020.",
year = "2020",
doi = "10.1007/978-1-0716-0680-3_9",
language = "English (US)",
series = "Methods in Molecular Biology",
publisher = "Humana Press",
pages = "101--113",
booktitle = "Methods in Molecular Biology",
}