Pseudo-contact shifts in the NMR spectrum of an entire paramagnetic catalytic metalloprotein domain

Together with international cooperation partners in Oulu and Florence, the Kaupp group in UniCat has shown, that the long-range pseudo-contact shifts in the NMR spectrum of an entire paramagnetic catalytic metalloprotein domain can be computed with a multi-scale approach based on ab initio methods. Using the trick of a point-dipole approximation for the long-range anisotropic hyperfine couplings, one can avoid having to compute the entire protein quantum-chemically but nevertheless obtains all the hundreds of long-range shifts. This even allowed the authors to go beyond DFT-methods and use high-level multi-reference ab initio methods. Due to the large structure sensitivity of the pseudo-contact shifts, this approach permits the refinement of both experimental and computed structural models of a metalloprotein, when the NMR shifts have been measured. This is a novel quantum-chemical tool for the determination of protein structures in combination with NMR measurements.

Original publication

Pseudo-contact NMR shifts over a paramagnetic metalloprotein (CoMMP-12) from first principles
L. Benda, J. Mareš, E. Ravera, G. Parigi, C. Luchinat, M. Kaupp, J. Vaara
Angew. Chem., Int. Ed. Engl. 2016, 55, 14713-14717
DOI: 10.1002/anie.201608829

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