Advertisement

Use of the Neutron Diffraction—H/D Exchange Technique to Determine the Conformational Dynamics of Trypsin

  • Anthony A. Kossiakoff
Chapter
Part of the Basic Life Sciences book series (BLSC, volume 27)

Abstract

A number of structural and chemical investigations (1–6) have shown that, even though protein molecules possess a high degree of secondary structure, they have numerous component segments which exhibit substantial fluctuations from their native conformations. A majority of these fluctuations represent a localized denaturation of small portions of the structure and result from the natural equilibrium between protein-protein and protein-solvent interactions. Although most of these fluctuations probably have little direct effect on the regions responsible for functional activity of the protein, a growing body of evidence indicates that conformational change is an important ingredient in a significant number of biological processes (7–10).

Keywords

Neutron Diffraction Amide Proton Regional Melting Peptide Proton Amide Peptide 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Linderstrom-Lang, K.U. and Schellman, J.A., in: “The Enzymes,” 2nd ed., P.D. Boyer et al., eds., Vol. 1, p. 443, Academic Press, New York (1959).Google Scholar
  2. 2.
    Gurd, F.N. and Rothgeb, T.M., Adv. Protein Chem. 33:73 (1979).PubMedCrossRefGoogle Scholar
  3. 3.
    Sternberg, M.J., Grace, D.E., and Phillips, D.C., J. Mol. Biol. 130:231 (1979).PubMedCrossRefGoogle Scholar
  4. 4.
    Frauenfelder, H., Petsko, G., and Tsernoglou, D., Nature (London) 280:558 (1979).CrossRefGoogle Scholar
  5. 5.
    McCammon, J.A., Gelin, B.R., and Karplus, M., Nature (London) 267:585 (1977).CrossRefGoogle Scholar
  6. 6.
    Karplus, M. and McCammon, J.A., CRC Crit. Rev. Biochem. 9:293 (1981).PubMedCrossRefGoogle Scholar
  7. 7.
    Lumry, R. and Biltonen, R., in: “Structure and Stability of Biological Macromolecules,” p. 65, Marcel Dekker, Inc., New York (1969).Google Scholar
  8. 8.
    Baldwin, R.L., Annu. Rev. Biochem. 44:453 (1975).PubMedCrossRefGoogle Scholar
  9. 9.
    Blumenfeld, L.A., J. Theor. Biol. 58:269 (1976).PubMedCrossRefGoogle Scholar
  10. 10.
    Welch, R.G., Somogyi, B., and Damjanovich, S., Prog. Biophys. Mol. Biol. 39:109 (1982).PubMedCrossRefGoogle Scholar
  11. 11.
    Hvidt, A. and Linderstrom-Lang, K., Biochim. Biophys. Acta 14:574 (1954).PubMedCrossRefGoogle Scholar
  12. 12.
    Hvidt, A., Johansen, G., and Linderstrom-Lang, K., in: “A Laboratory Manual of Analytical Techniques in Protein Chemistry,” P. Alexander and R.J. Block, eds., p. 101, Pergamon, New York (1960).Google Scholar
  13. 13.
    Hvidt, A. and Nielsen, S.O., Adv. Protein Chem. 21:287 (1966).PubMedCrossRefGoogle Scholar
  14. 14.
    Englander, S.W., Downer, N.W., and Teitelbaum, H., Annu. Rev. Biochem. 41:903 (1972).PubMedCrossRefGoogle Scholar
  15. 15.
    Englander, S.W., Calhoun, D.B., Englander, J.J., Kallenbach, N.R., Liem, H., Malin, E.L., Mandai, C., and Rogero, J.R., Biophys. J. 32:557 (1980).CrossRefGoogle Scholar
  16. 16.
    Woodward, C.K. and Hilton, B.D., Annu. Rev. Biophys. Bioeng. 8:99 (1979).PubMedCrossRefGoogle Scholar
  17. 17.
    Lumry, R. and Rosenberg, A., Colloq. Int. C.N.R.S. 246:53 (1975).Google Scholar
  18. 18.
    Richards, F.M., Carlsberg Res. Commun. 44:47 (1979).CrossRefGoogle Scholar
  19. 19.
    Wuthrich, K. and Wagner, G., J. Mol. Biol. 130:1 (1979).PubMedCrossRefGoogle Scholar
  20. 20.
    Wagner, G. and Wuthrich, K., J. Mol. Biol. 134:75 (1979).PubMedCrossRefGoogle Scholar
  21. 21.
    Hilton, B.D. and Woodward, C.K., Biochemistry 17:3325 (1978).PubMedCrossRefGoogle Scholar
  22. 22.
    Schreier, A.A. and Baldwin, R.L., J. Mol. Biol. 105:409 (1976).PubMedCrossRefGoogle Scholar
  23. 23.
    Rosa, J.J. and Richards, F.M., J. Mol. Biol. 133:399 (1979).PubMedCrossRefGoogle Scholar
  24. 24.
    Schoenborn, B.P., in: “Structure and Function of Oxidation Reduction Enzymes,” A. Akeson and A. Ehreberg, eds., p. 109, Pergamon, New York (1972).Google Scholar
  25. 25.
    Hanson, J.C. and Schoenborn, B.P., J. Mol. Biol. 153:117 (1981).PubMedCrossRefGoogle Scholar
  26. 26.
    Wlodawer, A. and Sjölin, L., Proc. Natl. Acad. Sci. USA 79:1418 (1982).PubMedCrossRefGoogle Scholar
  27. 27.
    Kossiakoff, A.A., Nature (London) 296:713 (1982).CrossRefGoogle Scholar
  28. 28.
    Mason, S.A., Bentley, G.A., and McIntyre, G.J., See paper in this Symposium.Google Scholar
  29. 29.
    Phillips, S.T.V., See paper in this Symposium.Google Scholar
  30. 30.
    Rupley, J.A., in: “Structure and Stability of Biological Macromolecules,” p. 291, Marcel Dekker, Inc., New York (1969).Google Scholar
  31. 31.
    Haggis, G.H., Biochim. Biophys. Acta 23:494 (1957).PubMedCrossRefGoogle Scholar
  32. 32.
    Praissman, M. and Rupley, J.A., Biochemistry 7:2431 (1968).PubMedCrossRefGoogle Scholar
  33. 33.
    Praissman, M. and Rupley, J.A., Biochemistry 7:2446 (1968).PubMedCrossRefGoogle Scholar
  34. 34.
    Tuchsen, E., Hvidt, A., and Ottesen, M., Biochimie 62:563 (1980).PubMedCrossRefGoogle Scholar
  35. 35.
    Perutz, M.F., Trans. Faraday Soc. B42:187 (1946).CrossRefGoogle Scholar
  36. 36.
    Low, B., Richards, F.M., and Berger, J.E., J. Am. Chem. Soc. 78:1107 (1956).CrossRefGoogle Scholar
  37. 37.
    Kossiakoff, A.A. and Spencer, S.A., Biochemistry 20:6462 (1981).PubMedCrossRefGoogle Scholar
  38. 38.
    Salemme, F.R., J. Mol. Biol. 146:143 (1981).PubMedCrossRefGoogle Scholar
  39. 39.
    Rose, G.D. and Roy, S., Proc. Natl. Acad. Sci. USA 77:4643 (1980).PubMedCrossRefGoogle Scholar
  40. 40.
    Artymiuk, P.J., Blake, C.C., Grace, D.E., Oatley, S.J., Phillips, D.C., and Sternberg, M.J., Nature (London) 28:563 (1979).CrossRefGoogle Scholar
  41. 41.
    Richardson, J.S., Adv. Protein Chem. 34:167 (1981).PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1984

Authors and Affiliations

  • Anthony A. Kossiakoff
    • 1
  1. 1.Brookhaven National LaboratoryUptonUSA

Personalised recommendations