Supramolecular Interactions Probed by 13C-13C Solid-State NMR Spectroscopy

We present a robust solid-state NMR approach for the accurate determination of molecular interfaces in insoluble and noncrystalline protein protein complexes. The method relies on the measurement of intermolecular C-13-C-13 distances in mixtures of [1-C-13]glucose- and [2-C-13]glucose-labeled proteins. We have applied this method to Parkinson's disease-associated a-synuclein fibrils and found that they are stacked in a parallel in-register arrangement. Additionally, intermolecular distance restraints for the structure determination of the fibrils at atomic resolution were measured.