NMR structural studies of glutathione S-transferase

Abstract.

The use of nuclear magnetic resonance (NMR) spectroscopy for the structure determination of small proteins is now widely recognized; what is less frequently reported is the application of NMR techniques for high-resolution studies of large proteins (M _r larger than 30 kD). We demonstrate here how an integrated approach, using heteronuclear NMR and X-ray crystallography, can provide useful and biologically important information for large protein systems. The dynamic features of the human A1-1 glutathione S-tranferase and the role of the C-terminal region are being probed by NMR; in the X-ray crystal structure, the electron densities for this region of the protein are uninterpretable.