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Deuterium Exchange in Lysozyme at 1.4-Å Resolution

  • Sax A. Mason
  • Graham A. Bentley
  • Garry J. McIntyre
Chapter
Part of the Basic Life Sciences book series (BLSC, volume 27)

Abstract

Hen egg-white lysozyme, the most widely studied of the chicken-type lysozymes, is an enzyme containing 129 amino acid residues, and it has been prepared in at least seven crystalline forms. The mechanism of action of lysozyme in cleaving the muco-polysaccharides of certain bacterial cell walls is now well understood, largely as a result of crystallographic investigations; see Imoto et al. (5) for a review. While crystallographic work continues in several laboratories, some aspects of the way lysozyme works in solution have been reexamined or clarified, in particular by high resolution NMR work (3), quantum-chemical calculations (12), and molecular dynamics calculations (9).

Keywords

Backbone Amide Occupation Factor Deuterium Exchange Neutron Diffraction Data Neutron Data 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Bentley, G.A., Duée, E.D., Mason, S.A., and Nunes, A.C., J. Chim. Phys. 76:817 (1979).Google Scholar
  2. 2.
    Bentley, G.A. and Mason, S.A., Philos. Trans. R. Soc. London B290:505 (1980).Google Scholar
  3. 3.
    Blake, C.C.F., Grace, D.E.P., Johnson, L.N., Perkins, S.J., Phillips, D.C., Cassells, R., Dobson, C.M., Poulsen, F.M., and Williams, R.J.P., in: “Molecular Interactions and Activity in Proteins,” Ciba Found. Symp. 60 (New Series), pp. 137-85, Excerpta Medica (1978).Google Scholar
  4. 4.
    Hodsdon, J.M., Sieker, L.C., and Jensen, L.H., Am. Crystallogr. Assn. Abstr. 3:16 (1975).Google Scholar
  5. 5.
    Imoto, T., Johnson, L.N., North, A.C.T., Phillips, D.C., and Rupley, J.A., in: “The Enzymes,” Vol. 7, pp. 665–868, P.D. Boyer, ed., American Press, New York (1972).Google Scholar
  6. 6.
    Konnert, J.H., Acta Crystallogr. A32:614 (1976).Google Scholar
  7. 7.
    Konnert, J.H. and Hendrickson, W.A., Acta Crystallogr. A36:344 (1980).Google Scholar
  8. 8.
    Kossiakoff, A.A., Nature 296;713 (1982).PubMedCrossRefGoogle Scholar
  9. 9.
    McCammon, J.A., Gelin, B.R., Karplus, M., and Wolynes, P.G., Nature 262:325 (1976).PubMedCrossRefGoogle Scholar
  10. 10.
    Moult, J., Yonath, A., Traub, W., Smilansky, A., Podjarny, A., Rabinovich, D., and Saya, A., J. Mol. Biol. 100:179 (1976).PubMedCrossRefGoogle Scholar
  11. 11.
    Wagner, G. and Wütrich, K., J. Mol. Biol. 155:347 (1982).PubMedCrossRefGoogle Scholar
  12. 12.
    Warshel, A. and Levitt, M., J. Mol. Biol. 103:227 (1976).PubMedCrossRefGoogle Scholar
  13. 13.
    Wlodawer, A. and Hendrickson, W.A., Acta Crystallogr. A38:239 (1982).Google Scholar
  14. 14.
    Wlodawer, A. and Sjölin, L., Proc. Natl. Acad. Sci. USA 79:1418 (1982).PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1984

Authors and Affiliations

  • Sax A. Mason
    • 1
  • Graham A. Bentley
    • 1
    • 2
  • Garry J. McIntyre
    • 1
  1. 1.Institut Laue-LangevinGrenoble CedexFrance
  2. 2.EMBL Grenoble OutstationGrenoble CedexFrance

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