Fig. 2

From macroscopic measurements to microscopic mechanisms of protein aggregation. In a typical in vitro aggregation experiment, recombinant proteins are purified using a number of procedures, including fast protein liquid chromatography. Samples containing purified proteins are aliquoted with an amyloid-binding fluorophore in a low-bind multiwell plate. A plate reader tracks the time-dependent evolution of the overall fibril mass, and kinetic traces can be subsequently analyzed using chemical kinetics to resolve the mechanism of aggregation, as well as the effects of additive species, such as aggregation inhibitors. The reactive flux towards oligomeric species can be calculated using this approach [179]. Relative flux graphic reprinted from Staats et.al [179]. Created with biorender.com