Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelles.
- 1 January 2002
- journal article
- Published by Springer Nature in Journal of Biomolecular NMR
- Vol. 23 (4) , 289-301
- https://doi.org/10.1023/a:1020218419190
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Structure of outer membrane protein A transmembrane domain by NMR spectroscopy.Nature Structural & Molecular Biology, 2001
- Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micellesProceedings of the National Academy of Sciences, 2001
- Impact of Transverse Relaxation Optimized Spectroscopy (TROSY) on NMR as a technique in structural biologyQuarterly Reviews of Biophysics, 2000
- Transverse-Relaxation-Optimized (TROSY) Gradient-Enhanced Triple-Resonance NMR SpectroscopyJournal of Magnetic Resonance, 1999
- Improved sensitivity and coherence selection for [15N,1H]-TROSY elements in triple resonance experimentsJournal of Biomolecular NMR, 1999
- Efficient side-chain and backbone assignment in large proteins: application to tGCN5.Journal of Biomolecular NMR, 1999
- The second decade — into the third milleniumNature Structural & Molecular Biology, 1998
- Single Transition-to-single Transition Polarization Transfer (ST2-PT) in [15N,1H]-TROSYJournal of Biomolecular NMR, 1998
- Recommendations for the presentation of NMR structures of proteins and nucleic acids – IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR SpectroscopyJournal of Biomolecular NMR, 1998
- Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutionsJournal of Biomolecular NMR, 1992