By a News Reporter-Staff News Editor at Life Science Weekly -- A new study on Life Science Research is now available. According to news reporting out of Karlsruhe, Germany, by NewsRx editors, research stated, "Light-controlled modification of the fluorescence emission properties of proteins of the GFP family is of crucial importance for many imaging applications including superresolution microscopy. Here, we have studied the reversibly photoswitchable fluorescent protein mIrisGFP using optical spectroscopy."
Our news journalists obtained a quote from the research from the Institute of Applied Physics, "By analyzing the pH dependence of isomerization and protonation equilibria and the isomerization kinetics, we have obtained insight into the coupling of the chromophore to the surrounding protein moiety and a better understanding of the photoswitching mechanism. A different acid-base environment of the chromophore's protonating group in its two isomeric forms, which can be inferred from the x-ray structures of IrisFP, is key to the photoswitching function and ensures that isomerization and protonation are correlated. Amino acids near the chromophore, especially Glu212, rearrange upon isomerization, and Glu212 protonation modulates the chromophore pK(a). In mIrisGFP, the cis chromophore protonates in two steps, with pK(cis) of 5.3 and 6, which is much lower than pK(trans) (>10)."
According to the news editors, the research concluded: "Based on these results, we have put forward a mechanistic scheme that explains how the combination of isomeric and acid-base properties of the chromophore in its protein environment can produce negative and positive photoswitching modes."
For more information on this research see: Mechanistic insights into reversible photoactivation in proteins of the GFP family. Biophysical Journal, 2012;103(12):2521-31. (Elsevier - www.elsevier.com; Biophysical Journal - www.elsevier.com/wps/product/cws_home/716950)
Our news journalists report that additional information may be obtained by contacting S. Gayda, Institute of Applied Physics and Center for Functional Nanostructures, Karlsruhe Institute of Technology, Karlsruhe, Germany. Additional authors for this research include K. Nienhaus and G.U Nienhaus (see also Life Science Research).
Keywords for this news article include: Europe, Germany, Peptides, Proteins, Karlsruhe, Amino Acids, Life Science Research.
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