Shorthand for protein which has been uniformly 15N- and 13C-labelled.
NMR spectroscopy using two NMR-active nuclei. For proteins this usually means 1H hydrogen and 15N nitrogen. To do this the protein must be 15N-labelled.
Heteronuclear Single-Quantum Correlation
Magic Angle Spinning. Solid-state NMR samples are often rotated/spun at high speeds (8-25 kHz or more) around the so-called magic angle (54.7 degrees) relative to the static magnetic field of the NMR spectrometer. This eliminates strong dipolar couplings and sharpens the resonance lines. The alternative is to use samples in which the molecules are all aligned the same way relative to the static magnetic field (which can be done relatively straight forwardly for membrane proteins).
Nuclear Magnetic Resonance (spectroscopy)
Nuclear Overhauser Effect (or Enhancement)
Nuclear Overhauser Effect (or Enhancement) Spectroscopy, usually refers to an NMR experiment which incorporates an element using the NOE
Residual Dipolar Coupling
All the spins belonging to the same residue
Shorthand for protein which has been uniformly 15N-, 13C- and 2H-labelled.
NMR spectroscopy using three NMR-active nuclei. For proteins this usually means 1H hydrogen, 15N nitrogen and 13C carbon. To do this the protein must be 15N- and 13C-labelled. Note that for triple resonance spectroscopy you need double labelled protein!