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Biophys. J. BioFAST: First Published January 28, 2005. doi:10.1529/biophysj.104.055541
© 2005 by the Biophysical Society.

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BIOPHYSICAL THEORY AND MODELING

Proton pathways in green fluorescence protein

Noam Agmon 1*

1 Hebrew University of Jerusalem

* To whom correspondence should be addressed. E-mail: agmon{at}fh.huji.ac.il.

Submitted on November 1, 2004
Revised on December 21, 2004
Accepted on 18 January 2005


  Abstract
Proton pathways in green fluorescent protein (GFP) are more extended than previously reported. In the x-ray data of wild-type GFP, a two-step exit pathway exists from the active site to the protein surface, controlled by a threonine switch. A proton entry pathwaybegins at a glutamate-lysine cluster around Glu5, and extends all the way to the buried Glu222 near the active site. These structural evidence suggest that GFP may function as a portable light drivenproton-pump, with proton emitted in the excited state through the switchable exit pathway, and replenished from Glu222 and the Glu5 entry pathway in the ground state.

Key Words: excited state proton transfer, green fluorescent protein (GFP), proton wire




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Copyright © 2005 by the Biophysical Society.