The conformational dynamics of intrinsically disordered proteins (IDP's) are inextricably linked to their roles in signaling, regulation, folding, and diseases. Single-molecule methods can contribute valuable information on the conformational dynamics of these biomolecules because they allow the observation of unsynchronized dynamics. Typically, target biomolecules are immobilized to allow study over a longer time window. However, biomolecules with more fluid structures, like IDP's, are highly susceptible to having their structure dominated by the immobilization environment. A method of studying single solution-phase biomolecules for prolonged periods of time would be highly useful for elucidating protein dynamics over many timescales.In this study, we present the use of a microfluidic trap that is capable of canceling Brownian motion to allow the observation of solution-phase dynamics of IDP's over multiple seconds. Two target families of biomolecules will be discussed: Tau, a protein contributor to the etiology of Alzheimer's disease, and nascent peptide-ribosome constructs that have been arrested before the completion of translation. The details of the technique, dynamics of the biomolecule targets, and future applications and directions will be discussed.

Conformational dynamics of intrinsically disordered proteins, one molecule at a time, studied with a microfluidic trap that cancels Brownian motion

247th National Meeting (2014)

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