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.
| Original language | English |
|---|---|
| Pages (from-to) | 359-362 |
| Number of pages | 3 |
| Journal | Cellular and Molecular Life Sciences |
| Volume | 54 |
| Issue number | 4 |
| Publication status | Published - 1998 |
Keywords
- Conformational changes
- Dynamics
- Glutathione S-transferase
- High resolution
- Isotopic labelling
- NMR
- Phenylalanines