Abstract

A metal ion with magnetic anisotropy in a biomolecule exerts strong paramagnetic effects on the nucleus spins of biomolecules in the NMR spectrum. The paramagnetic effects including paramagnetic relaxation enhancement (PRE), pseudocontact shift (PCS) and residual dipolar coupling (RDC) are valuable structural and dynamic restraints of biomolecules, and generation of these paramagnetic effects is a prerequisite. The susceptibility of magnetic anisotropy plays a similar role in the alignment of biomolecules to the commonly used alignment media in an external magnetic field. We summarize the strategies available for generating RDCs in proteins by paramagnetic labeling, selection of paramagnetic ions, and the factors influencing the magnitude of RDCs.

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