113Cd-1H heteroTOCSY: a method for determining metal-protein connectivities.
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 (heteroTOCSY) as viable alternatives. Additionally, we couple heteroTOCSY 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.
Gardner
K H
KH
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114.
Coleman
J E
JE
D002104:Cadmium; D007554:Isotopes; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008667:Metalloproteins / Q000737:chemistry*; D015394:Molecular Structure; D014157:Transcription Factors / Q000737:chemistry*
D007554:Isotopes; D008667:Metalloproteins; D014157:Transcription Factors; D002104:Cadmium