Fast assignments of 15N-HSQC spectra of proteins by paramagnetic labeling

Authors

Guido Pintacuda, Australian National University
Thomas Huber, University Of Queensland
Max A Keniry, Australian National University
Ah-Young Park, Australian National University
Nicholas E. Dixon, University of WollongongFollow
Gottfried Otting, Australian National University

RIS ID

16862

Publication Details

Pintacuda, G., Huber, T., Keniry, M., Park, A., Dixon, N. E. & Otting, G. (2006). Fast assignments of 15N-HSQC spectra of proteins by paramagnetic labeling. In G. A. Webb (Eds.), Modern Magnetic Resonance, Vol. 2 (pp. 1245-1250). Netherlands: Springer.

Abstract

¹⁵N-HSQC spectra of ¹⁵N-labeled proteins are widely used to identify ligand-binding sites on protein surfaces, providing a way to assess protein-protein interactions as well as to screen for the binding of small chemical compounds. The method is particularly powerful if the cross peaks in the ¹⁵N-HSQC spectrum have been sequence - specifically assigned. The present article reviews the use of paramagnetic labeling to obtain these resonance as- signments quickly with the use of ¹⁵N-labeled protein, provided the crystal structure of the protein is known and the protein can be labeled with a paramagnetic ion. The method also yields the anisotropy tensor of the magnetic susceptibility, which can be used to model the orientation of the ligand with respect to the protein.