NMR structural studies of glutathione S-transferase |
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Authors: | L-Y Lian |
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Institution: | (1) Biological NMR Centre, P.O. Box 138, Maurice Shock Medical Sciences Building, University of Leicester, Leicester LE1 9HN (UK), Fax +44 116 2523013, e-mail: yun@leicester.ac.uk, GB |
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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. |
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Keywords: | , Glutathione S-transferase, NMR, high resolution, phenylalanines, isotopic labelling, conformational changes, dynamics, |
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