Obtaining geometric snapshots of a protein as it folds will yield insights into how proteins achieve their unique
functional native 3-dimensional structure. Time-resolved FRET and time-resolved anisotropy are valuable tools toward
obtaining information about site-specific distances and side-chain mobility of the transient structures formed within
microseconds of initiating protein folding. To access this timescale we have merged dual-channel TCSPC detection with
recently developed laser-micromachining based microsecond turbulent mixer technology to obtain site-specific distance
information and rotational correlation times of protein folding intermediates in the 30 microsecond to seconds timescale.
Application of this approach shows that chain collapse to globular structures can occur in the several microsecond
timescale even for large proteins.
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