Heteronuclear NMR Studies of the Molecular Dynamics of Staphylococcal Nuclease

  • Dennis A. Torchia
  • Linda K. Nicholson
  • Holly B. R. Cole
  • Lewis E. Kay
Part of the Topics in Molecular and Structural Biology book series (TMSB)


During the past decade tremendous progress has been made in developing NMR techniques to determine the structure of proteins in solution. For proteins containing less than c. 100 residues, essentially complete proton signal assignments can be obtained using two- and three-dimensional homonuclear (proton) pulse sequences (Wüthrich, 1986; Clore and Gronenborn, 1989). These assignments together with distance and dihedral angle constraints, derived from NOEs and coupling constants, respectively, provide sufficient information to determine the three-dimensional structure of the protein. Recently it has been shown that NMR methods can be applied to larger proteins, containing up to c. 200 residues, by combining heteronuclear labelling (with 13C and/or 15N) with sophisticated double- and triple-resonance multidimensional techniques (Bax et al., 1990; Fesik et al., 1990; Ikura et al., 1990; Kay et al., 1990a,b; Clore et al., 1991a,b; Pelton et al., 1991).


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Copyright information

© The contributors 1993

Authors and Affiliations

  • Dennis A. Torchia
  • Linda K. Nicholson
  • Holly B. R. Cole
  • Lewis E. Kay

There are no affiliations available

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