Conformational freedom of the chromophore in fluorescent proteins

Kata A. Franczyk; Nathan P. Lemay; Scott L. Maddalo; Curran Mbofana; Marc Zimmer; Gabriel L. Chandler

doi:10.1117/12.702073

14 February 2007 Conformational freedom of the chromophore in fluorescent proteins

Kata A. Franczyk, Nathan P. Lemay, Scott L. Maddalo, Curran Mbofana, Marc Zimmer, Gabriel L. Chandler

Author Affiliations +

Proceedings Volume 6449, Genetically Engineered and Optical Probes for Biomedical Applications IV; 64490Q (2007) https://doi.org/10.1117/12.702073
Event: SPIE BiOS, 2007, San Jose, California, United States

Abstract

GFP is extensively used in molecular imaging applications. Its fluorescence is due to a autocatalytically formed chromophore located in the center of the protein. Yellow and blue fluorescent mutants of GFP have been created. The protein matrix that surrounds the chromophore influences both the intensity and the wavelength of the fluorescence. We have used conformational searching methods and molecular dynamics simulations to examine the &tgr; and &fgr; dihedral space available to a freely rotating and pyramidalizing chromophore. The calculations have shown that there seems to be a relationship between the quantum yield of the fluorescent protein and the dihedral &tgr; and &fgr; space available to the chromophore. The bright YFP has less rotational space available to a freely rotating chromophore than does wild-type GFP or BFP, which has the most rotational freedom.

Citation Download Citation

Kata A. Franczyk, Nathan P. Lemay, Scott L. Maddalo, Curran Mbofana, Marc Zimmer, and Gabriel L. Chandler "Conformational freedom of the chromophore in fluorescent proteins", Proc. SPIE 6449, Genetically Engineered and Optical Probes for Biomedical Applications IV, 64490Q (14 February 2007); https://doi.org/10.1117/12.702073

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KEYWORDS

Chromophores

Green fluorescent protein

Proteins

Luminescence

Fluorescent proteins

Crystals

Monte Carlo methods

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