Magnetic resonance spectroscopies can provide unique contributions to describe cellular processes. Magnetic resonance is indeed suitable not only for characterizing the structural and dynamical properties of biomolecules but, even more importantly, for describing transient interactions and functional events with atomic resolution possibly in a cellular context. This requires the development of suitable methodologies capable of addressing multiple, specific, and sometimes non conventional aspects for describing functional processes in cells.
I will present some examples on how NMR, also integrated with other techniques, can contribute to advance the knowledge on functional cellular processes. They often involve transient interactions suitably studied by NMR, which can also characterize processes in living cells with atomic resolution. Transient interactions occur in metal transfer processes1. The presence of paramagnetic centers, such as iron-sulfur clusters, dramatically affects the NMR spectra, requiring the development of tailored experiments and the integration with multiple techniques, with EPR being essential for these systems. The power of NMR in describing cellular pathways will be presented for processes responsible for copper trafficking and for the biogenesis of iron-sulfur proteins. New major advancements in in-cell NMR2,3 and in the characterization of highly paramagnetic systems4 will be also discussed within an integrated approach where, from single structures to protein complexes, the processes are described in their cellular context within a molecular perspective.
1 Banci L, et al. Affinity gradients drive copper to cellular destinations. Nature 465: 645-648, 2010
2 Banci, L., et al. Atomic-resolution monitoring of protein maturation in live human cells. Nat.Chem.Biol. 9, 297-299, 2013.
3 Luchinat E, Banci L. In-Cell NMR in Human Cells: Direct Protein Expression Allows Structural Studies of Protein Folding and Maturation. Acc Chem Res. 51, 1550-1557, 2018.
4 Banci L, et al. The NMR contribution to protein-protein networking in Fe-S protein maturation. J Biol Inorg Chem. 23, 665-685, 2018