We will use time-resolved SANS measurements to follow the self-assembly kinetics of insulin from protein monomers to fibrils. By measuring through a well-defined lag phase we hope to be able to directly observe the formation of the initial oligomeric structure that has been implicated as the toxic species in amyloid disease causing proteins. We aim to correlate the structural evolution of the fibrils to existing kinetic measurements that monitor the binding of a fluorescent dye to misfolded protein to see if the origin of the variability in the final state of these fluorescence measurements can be explained by variability in the fibrillar structure. By making measurements across a wide Q-range, we will be able to distinguish between different models for the fibril structure and to determine if aggregate formation is preceded by a peak in S(Q) of protein monomers.