Revealing the Affinity of Individual and Combined FliG Domains for FliM in the Bacterial Flagellar Motor Complex

Complex interactions between proteins modulate the rotational direction of bacterial flagella. This application note extends previous nuclear magnetic resonance (NMR) studies of the interactions between FliG domains with FliM via composition-gradient multi-angle static light scattering (CGMALS) to confirm specific binding, quantify affinities, and identify the stoichiometries of complexes formed.