Journal of Biomolecular NMR

, Volume 4, Issue 6, pp 761–774 | Cite as

113Cd-1H hetero TOCSY: A method for determining metal—protein connectivities

  • Kevin H. Gardner
  • Joseph E. Coleman
Research Paper

Summary

113Cd-1H NMR correlation experiments have been extremely useful for determining the amino acid ligands that form metal-binding sites in proteins. To date, the majority of these methods have used heteronuclear multiple-quantum transfer as the basis for establishing correlations. In this paper, we demonstrate the feasibility of using correlation methods that employ heteronuclear cross-polarization (hetero TOCSY) as viable alternatives. Additionally, we couple hetero TOCSY with selective excitation and transfer procedures to take advantage of the small number of heteronuclei usually present in metalloprotein systems. One- and two-dimensional experiments are presented as examples of these techniques.

Keywords

NMR Metalloproteins 113Cd Heteronuclear cross-polarization Hetero TOCSY 

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Copyright information

© ESCOM Science Publishers B.V 1994

Authors and Affiliations

  • Kevin H. Gardner
    • 1
  • Joseph E. Coleman
    • 1
  1. 1.Department of Molecular Biophysics and BiochemistryYale UniversityNew HavenU.S.A.

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