Related Experiment Video
Updated: Jul 2, 2026

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
Published on: January 5, 2024
Time-resolved dimerization of a PAS-LOV protein measured with photocoupled small angle X-ray scattering
Jessica S Lamb1, Brian D Zoltowski, Suzette A Pabit
1School of Applied and Engineering Physics and Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA.
Abstract:
Time-resolved small-angle X-ray scattering (SAXS) has been used to probe photoexcitation of the blue-light signal transduction protein Vivid (VVD). Laser excitation of sample in a continuous flow cell enables time-resolved measurement of the initial response of VVD to illumination. Good signal-to-noise is achieved without relying on multiple exposures of the same sample or limiting exposure times to prevent radiation damage. The SAXS data demonstrate that VVD dimerizes within tens of milliseconds of light-state activation. Time-resolved SAXS in a flow cell format is a general method for connecting chemical changes in photoreceptors to conformationally driven output signals.
More Related Videos
07:56Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time
Published on: May 30, 2021
10:03Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014