Thread: NMR paper Exploring Sulfur Sites in Proteins via Triple-Resonance 1H-Detected 77Se NMR
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Default Exploring Sulfur Sites in Proteins via Triple-Resonance 1H-Detected 77Se NMR
Exploring Sulfur Sites in Proteins via Triple-Resonance 1H-Detected 77Se NMR

NMR spectroscopy has been applied to virtually all sites within proteins and biomolecules; however, the observation of sulfur sites remains very challenging. Recent studies have examined ^(77)Se as a replacement for sulfur and applied ^(77)Se NMR in both the solution and solid states. As a spin-1/2 nuclide, ^(77)Se is attractive as a probe of sulfur sites, and it has a very large chemical shift range (due to a large chemical shift anisotropy), which makes it potentially very sensitive to...

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