Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/28507
Title: Screening protein – Single stranded RNA complexes by NMR spectroscopy for structure determination
Authors: Foot, Jaelle N.
Feracci, Mikael
Dominguez, Cyril
First Published: 1-Oct-2013
Publisher: Elsevier on behalf of Academic Press
Citation: Methods, 2014, 65 (3), pp. 288-301
Abstract: In the past few years, RNA molecules have been revealed to be at the center of numerous biological processes. Long considered as passive molecules transferring genetic information from DNA to proteins, it is now well established that RNA molecules play important regulatory roles. Associated with that, the number of identified RNA binding proteins (RBPs) has increased considerably and mutations in RNA molecules or RBP have been shown to cause various diseases, such as cancers. It is therefore crucial to understand at the molecular level how these proteins specifically recognise their RNA targets in order to design new generation drug therapies targeting protein–RNA complexes. Nuclear magnetic resonance (NMR) is a particularly well-suited technique to study such protein–RNA complexes at the atomic level and can provide valuable information for new drug discovery programs. In this article, we describe the NMR strategy that we and other laboratories use for screening optimal conditions necessary for structural studies of protein-single stranded RNA complexes, using two proteins, Sam68 and T-STAR, as examples.
DOI Link: 10.1016/j.ymeth.2013.09.018
ISSN: 1046-2023
eISSN: 1095-9130
Links: http://hdl.handle.net/2381/28507
http://www.sciencedirect.com/science/article/pii/S1046202313003873
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © 2013 The Authors. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Appears in Collections:Published Articles, Dept. of Biochemistry

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