Triple-resonance solid-state NMR assignment of protein spectra

We establish a method for assigning protein magic-angle spinning (MAS) NMR spectra that is based on tripleresonance techniques. It relies on perdeuteration, amide 2H/1H exchange, high magnetic fields, fast MAS, and enables automated assignment. The method is validated with examples covering microcrystalline proteins, a virus capsid and membrane-embedded systems. It eases and accelerates the assignment process, enabling NMR characterization of previously inaccessible biomolecules.