NMR Assignment and Secondary Structure Determination of an Octameric 110 kDa Protein Using TROSY in Triple Resonance Experiments
- 21 July 2000
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 122 (31) , 7543-7548
- https://doi.org/10.1021/ja0003268
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Polarization transfer by cross-correlated relaxation in solution NMR with very large moleculesProceedings of the National Academy of Sciences, 1999
- TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteinsProceedings of the National Academy of Sciences, 1998
- The second decade — into the third milleniumNature Structural & Molecular Biology, 1998
- Technical aspects of NMR Spectroscopy with biological macromolecules and studies of hydration in solutionProgress in Nuclear Magnetic Resonance Spectroscopy, 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
- Discovering High-Affinity Ligands for Proteins: SAR by NMRScience, 1996
- Protein Hydration in Aqueous SolutionScience, 1991
- Empirical correlation between protein backbone conformation and C.alpha. and C.beta. 13C nuclear magnetic resonance chemical shiftsJournal of the American Chemical Society, 1991
- NMR with Proteins and Nucleic AcidsEurophysics News, 1986
- Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonanceJournal of Molecular Biology, 1982