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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
