A novel protocol based on HN(C)N for rapid resonance assignment in (15N, 13C) labeled proteins: implications to structural genomics
- 1 April 2002
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 293 (1) , 427-432
- https://doi.org/10.1016/s0006-291x(02)00240-1
Abstract
No abstract availableKeywords
This publication has 7 references indexed in Scilit:
- An Efficient High-Throughput Resonance Assignment Procedure for Structural Genomics and Protein Folding Research by NMRBiochemistry, 2001
- Improved 3D triple resonance experiments, HNN and HN(C)N, for HN and 15N sequential correlations in (13C, 15N) labeled proteins: Application to unfolded proteinsJournal of Biomolecular NMR, 2001
- NMR spectroscopy: a multifaceted approach to macromolecular structureQuarterly Reviews of Biophysics, 2000
- 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
- Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMRJournal of the American Chemical Society, 1992
- Proton and nitrogen sequential assignments and secondary structure determination of the human FK506 and rapamycin binding proteinBiochemistry, 1991
- Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopyChemical Physics Letters, 1980