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Originally published as Biophys J. BioFAST on January 28, 2005.
doi:10.1529/biophysj.104.055541
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Biophysical Journal 88:2452-2461 (2005)
© 2005 The Biophysical Society

Proton Pathways in Green Fluorescence Protein

Noam Agmon

Department of Physical Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel

Correspondence: Address reprint requests to Noam Agmon, E-mail: agmon{at}fh.huji.ac.il.

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 pathway begins at a glutamate-lysine cluster around Glu-5, and extends all the way to the buried Glu-222 near the active site. This structural evidence suggests that GFP may function as a portable light-driven proton-pump, with proton emitted in the excited state through the switchable exit pathway, and replenished from Glu-222 and the Glu-5 entry pathway in the ground state.




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