Below is a Google-cached version of Protein NMR - A Practical Guide - Glossary / Abbreviations page from www.protein-nmr.org.uk crashed on 11/6/11. You may want to check first if the site has been restored since it would also display images or/and have a more updated info.
Glossary and Abbreviations
2D
two-dimensional
3D
three-dimensional
Double Labelled
Shorthand for protein which has been uniformly 15N- and 13C-labelled.
Double Resonance
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.
COSY
Correlation Spectroscopy
HSQC
Heteronuclear Single-Quantum Correlation
MAS
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).
NMR
Nuclear Magnetic Resonance (spectroscopy)
NOE
Nuclear Overhauser Effect (or Enhancement)
NOESY
Nuclear Overhauser Effect (or Enhancement) Spectroscopy, usually refers to an NMR experiment which incorporates an element using the NOE
RDC
Residual Dipolar Coupling
Spin System
All the spins belonging to the same residue
Triple Labelled
Shorthand for protein which has been uniformly 15N-, 13C- and 2H-labelled.
Triple Resonance
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!
