NMR structural studies of glutathione S-transferase

L. Y. Lian

    Research output: Contribution to journalArticlepeer-review


    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 languageEnglish
    Pages (from-to)359-362
    Number of pages3
    JournalCellular and Molecular Life Sciences
    Issue number4
    Publication statusPublished - 1998


    • Conformational changes
    • Dynamics
    • Glutathione S-transferase
    • High resolution
    • Isotopic labelling
    • NMR
    • Phenylalanines


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