II. Kinetic Pathways of Switching Optical Conformations in DsRed by 2D Fourier Imaging Correlation Spectroscopy

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-FI...

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Bibliographic Details
Published in:The journal of physical chemistry. B 2009-05, Vol.113 (19), p.6854-6860
Main Authors: Senning, Eric N, Lott, Geoffrey A, Fink, Michael C, Marcus, Andrew H
Format: Article
Language:English
Subjects:
Animals
B: Biophysical Chemistry
Color
Fourier Analysis
Kinetics
Luminescent Proteins - chemistry
Molecular Conformation
Optical Phenomena
Spectrum Analysis
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Summary: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 (10−3−102 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.
ISSN:1520-6106
1520-5207
DOI:10.1021/jp901542b