Modulating the pH dependent photophysical properties of green fluorescent protein.

The photophysical properties of the β-barrel superfolder green fluorescent protein (sfGFP) arise from the chromophore that forms post-translationally in the interior of the protein. Specifically, the protonation state of the side chain of tyrosine 66 in the chromophore, in addition to the network of hydrogen bonds between the chromophore and surrounding residues, is directly related to the electronic absorbance and emission properties of the protein. The pH dependence of the photophysical properties of this protein were modulated by the genetic, site-specific incorporation of 3-nitro-l-tyrosine (mNOY) at site 66 in sfGFP.

Monte Carlo Simulations Comparing the Response of a Novel Hemispherical Tepc to Existing Spherical and Cylindrical Tepcs for Neutron Monitoring and Dosimetry.

Neutron dosimetry in reactor fields is currently mainly conducted with unwieldy flux monitors. Tissue Equivalent Proportional Counters (TEPCs) have been shown to have the potential to improve the accuracy of neutron dosimetry in these fields, and Multi-Element Tissue Equivalent Proportional Counters (METEPCs) could reduce the size of instrumentation required to do so. Complexity of current METEPC designs has inhibited their use beyond research.