Four-dimensional heteronuclear triple-resonance NMR of isotopically enriched proteins for sequential assignment of backbone atoms
- 1 February 1991
- journal article
- research article
- Published by Elsevier in Journal of Magnetic Resonance (1969)
- Vol. 91 (2) , 422-428
- https://doi.org/10.1016/0022-2364(91)90208-b
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- Four-Dimensional Heteronuclear Triple-Resonance NMR Spectroscopy of Interleukin-1β in SolutionScience, 1990
- Identification and localization of bound internal water in the solution structure of interleukin 1.beta. by heteronuclear three-dimensional proton rotating-fram Overhauser nitrogen-15-proton multiple quantum coherence NMR spectroscopyBiochemistry, 1990
- Overcoming the overlap problem in the assignment of proton NMR spectra of larger proteins by use of three-dimensional heteronuclear proton-nitrogen-15 Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1.beta.Biochemistry, 1989
- Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5aBiochemistry, 1989
- Three-dimensional heteronuclear NMR of nitrogen-15 labeled proteinsJournal of the American Chemical Society, 1989
- A powerful method of sequential proton resonance assignment in proteins using relayed 15N‐1H multiple quantum coherence spectroscopyFEBS Letters, 1989
- Heteronuclear three-dimensional NMR spectroscopy. Natural abundance carbon-13 chemical shift editing of 1H-1H COSY spectraJournal of the American Chemical Society, 1989
- NOESY-TOCSY, an Advantageous 2D NMR Technique for the Analysis of Peptide SequencesAngewandte Chemie International Edition in English, 1988
- Three-dimensional NMR spectroscopy of a protein in solutionNature, 1988
- Toward the complete assignment of the carbon nuclear magnetic resonance spectrum of the basic pancreatic trypsin inhibitorBiochemistry, 1986