Abstract
The process of folding a polypeptide chain from an unstructured random coil in denaturant to a functional 3 dimensional form is a rapid process that is perhaps biased very early on during the initial steps, even as the solvent conditions are transitioning from favoring denaturation to favoring folding. Access to kinetics in the microseconds to milliseconds time scale by multiple spectroscopic probes is crucial to interpreting these initial steps of folding. Time resolved small angle X-ray scattering (trSAXS) is a powerful technique for studying 3 dimensional shapes of proteins as they transition from unfolded to native structures. By interfacing microfluidic devices with powerful x-ray sources we can access timescales in the sub-hundred microseconds range. Structural details determined using trSAXS of the kinetic refolding process of CheY reveal a burst phase in the sub 50-microsecond time-scale, that is perhaps structured around a local-in-sequence cluster of hydrophobic residues.
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