Article
Structure and excited-state proton transfer in the GFP S205A mutant.
The journal of physical chemistry. B - 20 Oct 2011
Erez Yuval, Gepshtein Rinat, Presiado Itay, Trujillo Kristina, Kallio Karen, Remington S James, Huppert Dan
Abstract excerpt
To further explore excited state proton transfer (ESPT) pathways within green fluorescent protein (GFP), mutagenesis, X-ray crystallography, and time-resolved and steady-state optical spectroscopy were employed to create and study the GFP mutant S205A. In wild type GFP (wt-GFP), the proton transfer pathway includes the hydroxyl group of the chromophore, a water molecule, Ser205, and Glu222. We found that the ESPT...
Topics
Join the communities discussing this publication.