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Proceedings Paper

Conformational freedom of the chromophore in fluorescent proteins
Author(s): Kata A. Franczyk; Nathan P. Lemay; Scott L. Maddalo; Curran Mbofana; Marc Zimmer; Gabriel L. Chandler
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Paper 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.

Paper Details

Date Published: 14 February 2007
PDF: 10 pages
Proc. SPIE 6449, Genetically Engineered and Optical Probes for Biomedical Applications IV, 64490Q (14 February 2007); doi: 10.1117/12.702073
Show Author Affiliations
Kata A. Franczyk, Connecticut College (United States)
Nathan P. Lemay, Connecticut College (United States)
Scott L. Maddalo, Connecticut College (United States)
Curran Mbofana, Connecticut College (United States)
Marc Zimmer, Connecticut College (United States)
Gabriel L. Chandler, Connecticut College (United States)

Published in SPIE Proceedings Vol. 6449:
Genetically Engineered and Optical Probes for Biomedical Applications IV
Samuel Achilefu; Alexander Pavlovich Savitsky; Rebekka M. Wachter; Darryl J. Bornhop; Ramesh Raghavachari, Editor(s)

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