ArticleJournal of the American Chemical Society2010
Intermediate rate atomic trajectories of RNA by solid-state NMR spectroscopy.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Investigation of biomolecular dynamics by sensitivity-enhancedJournal of magnetic resonance open · 2024Article
- Elucidating microRNA-34a organisation within human Argonaute-2 by dynamic nuclear polarisation-enhanced magic angle spinning NMR.Nucleic acids research · 2024Article
- Dynamics of base pairs with low stability in RNA by solid-state nuclear magnetic resonance exchange spectroscopy.iScience · 2022Article
- Nucleic acid-protein interfaces studied by MAS solid-state NMR spectroscopy.Journal of structural biology: X · 2022Article
- Strategies for RNA Resonance Assignment byFrontiers in molecular biosciences · 2021Review
- RNA Dynamics by NMR Spectroscopy.Chembiochem : a European journal of chemical biology · 2019Review
- Isotope labeling for studying RNA by solid-state NMR spectroscopy.Journal of biomolecular NMR · 2018Review
- Ultraslow Domain Motions in HIV-1 TAR RNA Revealed by Solid-State Deuterium NMR.The journal of physical chemistry. B · 2017Article
- Magic angle spinning NMR of viruses.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- NMR studies of dynamic biomolecular conformational ensembles.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- Molecular dynamics simulations identify time scale of conformational changes responsible for conformational selection in molecular recognition of HIV-1 transactivation responsive RNA.Journal of the American Chemical Society · 2014Article
- Efficient in silico exploration of RNA interhelical conformations using Euler angles and WExplore.Nucleic acids research · 2014Article
- Coarse grained models reveal essential contributions of topological constraints to the conformational free energy of RNA bulges.The journal of physical chemistry. B · 2014Article
- Elucidating molecular motion through structural and dynamic filters of energy-minimized conformer ensembles.The journal of physical chemistry. B · 2014Article
- Hierarchy of RNA functional dynamics.Annual review of biochemistry · 2014Review
- A general method for constructing atomic-resolution RNA ensembles using NMR residual dipolar couplings: the basis for interhelical motions revealed.Journal of the American Chemical Society · 2013Article
- Independent alignment of RNA for dynamic studies using residual dipolar couplings.Journal of biomolecular NMR · 2012Article
- New insights into the fundamental role of topological constraints as a determinant of two-way junction conformation.Nucleic acids research · 2012Article
- Intrinsic nucleic acid dynamics modulates HIV-1 nucleocapsid protein binding to its targets.PloS one · 2012Article
- Theory of nonrigid rotational motion applied to NMR relaxation in RNA.The journal of physical chemistry. A · 2011Article
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5 authors.
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Abstract
Many RNAs undergo large conformational changes in response to the binding of proteins and small molecules. However, when RNA functional dynamics occur in the nanosecond-microsecond time scale, they become invisible to traditional solution NMR relaxation methods. Residual dipolar coupling methods have revealed the presence of extensive nanosecond-microsecond domain motions in HIV-1 TAR RNA, but this technique lacks information on the rates of motions. We have used solid-state deuterium NMR to quantitatively describe trajectories of key residues in TAR by exploiting the sensitivity of this technique to motions that occur in the nanosecond-microsecond regime. Deuterium line shape and relaxation data were used to model motions of residues within the TAR binding interface. The resulting motional models indicate two functionally essential bases within the single-stranded bulge sample both the free and Tat-bound conformations on the microsecond time scale in the complete absence of the protein. Thus, our results strongly support a conformational capture mechanism for recognition: the protein does not induce a new RNA structure, but instead captures an already-populated conformation.
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