NMR structural studies of glutathione S-transferase.
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 Al-1 glutathione S-transferase 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.
Lian
L Y
LY
Biological NMR Centre, University of Leicester, UK. yun@leicester.ac.uk
D018360:Crystallography, X-Ray; D005982:Glutathione Transferase / Q000737:chemistry*; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular
D005982:Glutathione Transferase