A New Method To Detect Long-Range Protein−RNA Contacts: NMR Detection of Electron−Proton Relaxation Induced by Nitroxide Spin-Labeled RNA
- 1 October 1998
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 120 (42) , 10992-10993
- https://doi.org/10.1021/ja982496e
Abstract
No abstract availableThis publication has 9 references indexed in Scilit:
- RNA RECOGNITION BY RNP PROTEINS DURING RNA PROCESSINGAnnual Review of Biophysics, 1998
- Solution Structure of a DNA Duplex Containing a Nitroxide Spin-Labeled Platinum d(GpG) Intrastrand Cross-Link Refined with NMR-Derived Long-Range Electron−Proton Distance RestraintsJournal of the American Chemical Society, 1998
- Attenuated T 2 relaxation by mutual cancellation of dipole–dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solutionProceedings of the National Academy of Sciences, 1997
- Paramagnetic relaxation as a tool for solution structure determination:Clostridium pasteurianum ferredoxin as an exampleProteins-Structure Function and Bioinformatics, 1997
- RNA−Protein Intermolecular RecognitionAccounts of Chemical Research, 1997
- RNA—protein complexesCurrent Opinion in Structural Biology, 1996
- NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5.The EMBO Journal, 1995
- A conserved double-stranded RNA-binding domain.Proceedings of the National Academy of Sciences, 1992
- Heteronuclear filters in two-dimensional [1H, 1H]-NMR spectroscopy: combined use with isotope labelling for studies of macromolecular conformation and intermolecular interactionsQuarterly Reviews of Biophysics, 1990