ArticleJournal of biomolecular NMR2012
Independent alignment of RNA for dynamic studies using residual dipolar couplings.
Article in Journal of biomolecular NMR, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 11 citations in OpenAlex.
- More than Proton Detection-New Avenues for NMR Spectroscopy of RNA.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Review
- RNA Dynamics by NMR Spectroscopy.Chembiochem : a European journal of chemical biology · 2019Review
- Applications of NMR to structure determination of RNAs large and small.Archives of biochemistry and biophysics · 2017Review
- Structure of a low-population binding intermediate in protein-RNA recognition.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Structural Analysis of Multi-Helical RNAs by NMR-SAXS/WAXS: Application to the U4/U6 di-snRNA.Journal of molecular biology · 2016Article
- Modulating RNA Alignment Using Directional Dynamic Kinks: Application in Determining an Atomic-Resolution Ensemble for a Hairpin using NMR Residual Dipolar Couplings.Journal of the American Chemical Society · 2015Article
- Insights into domain-domain motions in proteins and RNA from solution NMR.Accounts of chemical research · 2014Review
- Elucidating molecular motion through structural and dynamic filters of energy-minimized conformer ensembles.The journal of physical chemistry. B · 2014Article
- Advances in the determination of nucleic acid conformational ensembles.Annual review of physical chemistry · 2014Review
- NMR studies of nucleic acid dynamics.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecular motion and dynamics play an essential role in the biological function of many RNAs. An important source of information on biomolecular motion can be found in residual dipolar couplings which contain dynamics information over the entire ms-ps timescale. However, these methods are not fully applicable to RNA because nucleic acid molecules tend to align in a highly collinear manner in different alignment media. As a consequence, information on dynamics that can be obtained with this method is limited. In order to overcome this limitation, we have generated a chimeric RNA containing both the wild type TAR RNA, the target of our investigation of dynamics, as well as the binding site for U1A protein. When U1A protein was bound to the portion of the chimeric RNA containing its binding site, we obtained independent alignment of TAR by exploiting the physical chemical characteristics of this protein. This technique can allow the extraction of new information on RNA dynamics, which is particularly important for time scales not covered by relaxation methods where important RNA motions occur.
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