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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Efficient chi-tensor determination and NH assignment of paramagnetic proteins.

Anisotropic magnetic susceptibility tensors chi of paramagnetic metal ions are manifested in pseudocontact shifts, residual dipolar couplings, and other paramagnetic observables that present valuable long-range information for structure determinations of protein-ligand complexes. A program was developed for automatic determination of the chi-tensor anisotropy parameters and amide resonance assignments in proteins labeled with paramagnetic metal ions. The program requires knowledge of the three-dimensional structure of the protein, the backbone resonance assignments of the diamagnetic protein, and a pair of 2D (15)N-HSQC or 3D HNCO spectra recorded with and without paramagnetic metal ion. It allows the determination of reliable chi-tensor anisotropy parameters from 2D spectra of uniformly (15)N-labeled proteins of fairly high molecular weight. Examples are shown for the 185-residue N-terminal domain of the subunit epsilon from E. coli DNA polymerase III in complex with the subunit theta and La(3+) in its diamagnetic and Dy(3+), Tb(3+), and Er(3+) in its paramagnetic form.[1]

References

  1. Efficient chi-tensor determination and NH assignment of paramagnetic proteins. Schmitz, C., John, M., Park, A.Y., Dixon, N.E., Otting, G., Pintacuda, G., Huber, T. J. Biomol. NMR (2006) [Pubmed]
 
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