title: Time-resolved dimerization of a PAS-LOV protein measured with photocoupled small angle X-ray scattering.
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.
authors: School of Applied and Engineering Physics and Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA.
authors: Jessica S
authors: JS
authors: Lamb
authors: Brian D
authors: BD
authors: Zoltowski
authors: Suzette A
authors: SA
authors: Pabit
authors: Brian R
authors: BR
authors: Crane
authors: Lois
authors: L
authors: Pollack
mesh_terms: D019281:Dimerization; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D010100:Oxygen / Q000737:chemistry / Q000378:metabolism; D010777:Photochemistry; D053838:Scattering, Small Angle; D014961:X-Ray Diffraction
chemical_list: D005656:Fungal Proteins; C423283:VVD protein, Neurospora crassa; D010100:Oxygen