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Determination of Macromolecular Structure and Dynamics by NMR

  • Oleg Jardetzky
  • Andrew Lane
  • Jean-Francois Lefevre
  • Olivier Lichtarge
  • Barbara Hayes-Roth
  • Bruce Buchanan
Part of the NATO ASI Series book series (NSSA, volume 107)

Abstract

The possibility of defining solution structures of proteins and nucleic acids from NMR data has been advanced for many years [1, 2, 3]. In several cases, partial successes have been achieved [4, 5, 6]. However, a closer examination of the lines of argument used in the interpretation of NMR data forces one to conclude that they have not led to the development of an independent, generally applicable method for this purpose. The most successful examples (5, 6) have relied heavily on prior knowledge of the crystal structure — or of very similar crystal structures — and/or on a priori additional constraints, such as the assumption that a single rigid structure exists in solution which can be calculated from the data by minimizing either an error function or the energy of the structure. The danger of such procedures has been discussed elsewhere [8, 9, 10].

Keywords

Free Volume Correlation Time Knowledge Source Twist Angle Internuclear Distance 
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.
    Jardetzky, O. (1965) Proc. Int. Conf. Mag. Res., Tokyo, Japan N-3–14: 1–4.Google Scholar
  2. 2.
    Campbell, I.D., Dobson, C.M., Williams, R.J.P. and Xavier, A.V. (1973) Ann. Rev. NY Acad. Sci. 222, 1963.Google Scholar
  3. 3.
    Wagner, G. and Wuthrich, K. (1982) J. Mol. Biol. 155, 427–466.CrossRefGoogle Scholar
  4. 4.
    Braun, W., Bosch, C., Brown, L.R., Go, N. and Wuthrich, K. (1981) Biochim. Biophys. Acta 667, 377.PubMedGoogle Scholar
  5. 5.
    Braun, W., Wider, G., Lee, K.H. and Wuthrich, K. (1983) J. Mol. Biol. 109, 921–948.CrossRefGoogle Scholar
  6. 6.
    Zuiderweg, E.R.P., Billeter, M., Boelens, R., Scheek, R.M., Wuthrich, K. and Kaptein, R. (1984) FEBS Lett 179, 243–247.CrossRefGoogle Scholar
  7. 7.
    Kaptein, R., Zuiderweg, E.R.P., Scheek, R.M. and Boelens, R. (1985) J. Mol. Biol. 182, 179–182.PubMedCrossRefGoogle Scholar
  8. 8.
    Jardetzky, O. (1980) Biochim. Biophys. Acta 621, 227–232.PubMedGoogle Scholar
  9. 9.
    Jardetzky, O. and Roberts, G.C.K. (1981) “NMR in Molecular Biology”, Academic Press, New York, Ch. 4.Google Scholar
  10. 10.
    Jardetzky, O. (1984) in “Progress in Bioorganic Chemistry and Molecular Biology”. Yu. A. Ovchinnikov, ed., Elsevier Science Publishers B.V., Amsterdam, pp. 55–63.Google Scholar
  11. 11.
    Kratky, O., Leopold, H. and Staubinger, H. (1973) Meths. Enzymol. 270, 98–110.CrossRefGoogle Scholar
  12. 12.
    McMeekin, T.L. and Marshall, K. (1952) Science 116, 142–144.PubMedCrossRefGoogle Scholar
  13. 13.
    Lane, A.N. and Kirschner, K. (1983) Eur. J. Biochem. 129, 675–684.PubMedCrossRefGoogle Scholar
  14. 14.
    Lane, A.N. (1982) J. Theor. Biol. 97, 511–527.PubMedCrossRefGoogle Scholar
  15. 15.
    Jardetzky, O. (1981) Accts. Chem. Res. 14, 291–298CrossRefGoogle Scholar
  16. 16.
    Lane, A.N. (1983) Eur. J. Biochem. 133. 531–538.PubMedCrossRefGoogle Scholar
  17. 17.
    Calhoun, P.B., Vanderkooi, J.M., Woodrow, G.V. and Englander, S.W. (1983) Biochem. 22, 1526–1532.CrossRefGoogle Scholar
  18. 18.
    Paul, C.H. (1982) J. Mol. Biol. 155, 53–62.PubMedCrossRefGoogle Scholar
  19. 19.
    Lane, A.N., Lefevre, J-F. and Jardetzky, O. (1985) submitted to J. Mag. Res.Google Scholar
  20. 20.
    van de Ven F.J.M.. de Bruin, S.N. and Hilbers, C.W. (1984) FEBS Lett. 169, 107–111.CrossRefGoogle Scholar
  21. 21.
    Jones, C.R., Sikakana, C.T., Henir, S.P., Kuo, M.C. and Gibbons W.A. (1978) Biophys. J. 24. 815–824.PubMedCrossRefGoogle Scholar
  22. 22.
    Jones C.R., Sikakana, C.T., Henir, S.P., Kuo, M.C. and Gibbons, W.A. (1978) J. Am. Chem. Soc. 100, 5960–5967.CrossRefGoogle Scholar
  23. 23.
    Billeter, M., Braun W. and Wuthrich, K. (1982) J. Mol. Biol. 155. 321–346.PubMedCrossRefGoogle Scholar
  24. 24.
    Zuiderweg, E.R.P., Kaptein, R. and Wuthrich, K. (1983) Proc. Natl. Acad. Sci. 80, 5837–5841.PubMedCrossRefGoogle Scholar
  25. 25.
    Molday, R.S., Englander, S.W. and Kallen, R.G. (1972) Biochem. 11, 150–161.CrossRefGoogle Scholar
  26. 26.
    Wagner, G. (1983) Q. Rev. Biophys. 16. 1–57.PubMedCrossRefGoogle Scholar
  27. 27.
    Hare, D.R., Wemmer, D.E., Chou S-H.. Drobny G. and Reid B.R. (1983) J. Mol. Biol. 171. 319–336.PubMedCrossRefGoogle Scholar
  28. 28.
    Richardson, J. (1980) in “Protein Folding”, Jaenicke, R., ed., Elsevier Science Publishers B.V., Amsterdam, pp. 41–52.Google Scholar
  29. 29.
    Finney, D. (1979) in “Water”, vol. 6, Franks, F.. ed., Plenum Press. New York, Ch. 2.Google Scholar
  30. 30.
    Bothner-By A.A. and Noggle J.H. (1979) J. Am. Chem. Soc. 101. 5162–5170.CrossRefGoogle Scholar
  31. 31.
    Saenger, W. (1984) “Principles of Nucleic Acid Structure”, Springer Verlag, New York.CrossRefGoogle Scholar
  32. 32.
    Fratini, A.V.. Kopka M.L., Drew H.R. and Dickerson R.E. (1982) J. Biol. Chem. 257. 14686–14707.PubMedGoogle Scholar
  33. 33.
    Calladine C.R. (1982) J. Mol. Biol. 161. 343–352.PubMedCrossRefGoogle Scholar
  34. 34.
    Lefevre J-F.. Lane, A.N. and Jardetzky O. (1985) in press FEBS Lett.Google Scholar

Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Oleg Jardetzky
    • 1
  • Andrew Lane
    • 1
  • Jean-Francois Lefevre
    • 1
  • Olivier Lichtarge
    • 1
  • Barbara Hayes-Roth
    • 2
  • Bruce Buchanan
    • 2
  1. 1.Stanford Magnetic Resonance LaboratoryUSA
  2. 2.Knowledge Systems Laboratory and Department of Computer ScienceStanford UniversityStanfordUSA

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