Abstract
The kinetics of biomolecular conformational transitions can be studied by two-dimensional (2D) magnetic resonance and optical spectroscopic methods. Here we apply polarization-modulated Fourier imaging correlation spectroscopy (PM-FICS) to demonstrate a new approach to 2D optical spectroscopy. PM-FICS enables measurements of conformational fluctuations of fluorescently labeled macromolecules on a broad range of time scales (10(-3)-10(2) s). We examine the optical switching pathways of DsRed, a tetrameric complex of fluorescent protein subunits. An analysis of PM-FICS coordinate trajectories, in terms of 2D spectra and joint probability distributions, provides detailed information about the transition pathways between distinct dipole-coupled DsRed conformations.
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.
