NMR Structural Studies of Flexible Molecules

  • Peter E. Wright
  • H. Jane Dyson


In recent years, NMR has been applied with great success to determine precise three- dimensional solution structures of compact globular proteins and small, inflexible cyclic peptides. NMR also holds promise for providing structural information on flexible biomolecules, although a quantitative description of structure is complicated by the inevitable population-weighted averaging of the key NMR parameters. Here we describe simple procedures for calculation of the dominant structure in the conformational ensemble of a linear peptide and for characterizing the domain motions and overall structural preferences of multidomain proteins.


Distance Constraint Linear Peptide Distance Geometry Conformational Ensemble Dihedral Angle Constraint 
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.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Billeter, M., Braun, W., & Wiithrich, K. (1982) Sequential resonance assignments in protein lVL nuclear magnetic resonance spectra. Computation of sterically allowed proton- proton distances and statistical analysis of proton-proton distances in single crystal protein conformations. J. Mol Biol 155, 321–346.PubMedCrossRefGoogle Scholar
  2. Briischweiler, R., Liao, X., & Wright, P.E. (1995) Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling. Science 268, 886–889.CrossRefGoogle Scholar
  3. Dyson, H.J., Ranee, M., Houghten, R.A., Lerner, R.A., & Wright, P.E. (1988) Folding of immunogenic peptide fragments of proteins in water solution. I Sequence requirements for the formation of a reverse turn. J. Mol Biol 201, 161–200.PubMedCrossRefGoogle Scholar
  4. Dyson, H.J. & Wright, P.E. (1991) Defining solution conformations of small linear peptides. Ann. Rev. Biophys. Biophys. Chem. 20, 519–538.CrossRefGoogle Scholar
  5. Havel, T.F. & Wuthrich, K. (1984) A distance geometry program for determining the structures of small proteins and other macromolecules from nuclear magnetic resonance measurements of intramolecular 1H-1H proximities in solution. Bull. Math. Biol 46, 73–698.Google Scholar
  6. Lee, M.S., Gippert, G., Soman, K.Y., Case, D.A., & Wright, P.E. (1989) Three-dimensional solution structure of a single zinc finger binding domain. Science 245, 635–637.PubMedCrossRefGoogle Scholar
  7. Liao, X., Clemens, K.R., Tennant, L., Wright, P.E., & Gottesfeld, J.M. (1992) Specific interaction of the first three zinc fingers of TFIIIA with the internal control region of the Xenopus 5S RNA gene. J. Mol Biol 223, 857–871.PubMedCrossRefGoogle Scholar
  8. Metzler, W.J., Hare, D.R., & Pardi, A. (1989) Limited sampling of conformational space by the distance geometry algorithm: Implications for structures generated from NMR data. Biochemistry 28, 7045–7052.PubMedCrossRefGoogle Scholar
  9. Palmer, A.G.,III, Ranee, M., & Wright, P.E. (1991) Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance 13C NMR spectroscopy. J. Am. Chem. Soc. 113,4371–4380.CrossRefGoogle Scholar
  10. Pearlman, D.A., Case, D.A., Caldwell, J.W., Ross, W.S., Cheatham, T.E.,III, Ferguson, D.M., Seibel, G.L., Singh, U.C., Weiner, P.K., & Kollman, P.A. (1995) AMBER 4.1, University of California, San Francisco.Google Scholar
  11. Richardson, J.S. & Richardson, D.C. (1989) Principles and patterns of protein conformation, in Prediction of Protein Structure and the Principles of Protein Conformation (Fasman, G.D. Ed.) Plenum Press, New York., pp 1–99Google Scholar
  12. Weiner, S.J., Kollman, P.A., Nguyen, D.T., & Case, D.A. (1986) An all atom force field for simulations of proteins and nucleic acids. J. Computat. Chem. 7, 230–252.CrossRefGoogle Scholar
  13. Woessner, D.E. (1962) Spin relaxation processes in a two-proton system undergoing anisotropic reorientation. J. Chem. Phys. 36, 1–4.CrossRefGoogle Scholar
  14. Yao, J., Feher, V.A., Espejo, B.F., Reymond, M.T., Wright, P.E., & Dyson, H.J. (1994a) Stabilization of a Type VI turn in a family of linear peptides in water solution. J. Mol Biol 243, 736–753.PubMedCrossRefGoogle Scholar
  15. Yao, J., Dyson, H.J., & Wright, P.E. (1994b) Three-dimensional structure of a Type VI turn in a linear peptide in water solution: evidence for stacking of aromatic rings as a major stabilizing factor. J. Mol Biol 243, 754–766PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1996

Authors and Affiliations

  • Peter E. Wright
    • 1
  • H. Jane Dyson
    • 1
  1. 1.Department of Molecular BiologyThe Scripps Research InstituteLa JollaUSA

Personalised recommendations