Over the past several years, microfluidic mixers with a variety of spectroscopic probes have been used to examine protein folding on the microsecond timescale under strong folding conditions that had not been previously accessible.  Many of these measurements have yielded surprising results, including unexpected kinetic processes, kinetics that depend on the measurement probe and kinetics that depend on the starting conditions.  This observed complexity usually cannot be explained by simple two- or three-state models.  In this talk I will highlight some of our recent results on proteins such as lambda repressor, villin, and ACBP and the models of varying complexity we have used to explain them.  I will also describe our newest methods to determine structure formation.

Using microfluidic mixers to measure protein structure formation

243rd National Meeting (2012)

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