A new approch for structure determination of proteins by three-dimensional NMR.
1992
Recent development of three-dimensional (3D) nuclear magnetic resonance (NMR) spectroscopy offers a new sight into the determination of the structures of larger proteins by increasing spectral resolution in three frequency axes. Simultaneously, problems of sensitivity loss due to larger linewidths associated with the increase of molecular weights has been solved by use of large three-dimensional NMR/protein structure/triple-resonance NMR/stable isotope
Keywords:
- Nuclear magnetic resonance spectroscopy
- Triple-resonance nuclear magnetic resonance spectroscopy
- Fluorine-19 NMR
- Carbon-13 NMR satellite
- Nuclear magnetic resonance crystallography
- Carbon-13 NMR
- Two-dimensional nuclear magnetic resonance spectroscopy
- Nuclear magnetic resonance
- Transverse relaxation-optimized spectroscopy
- Chemistry
- Analytical chemistry
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