Russell B Vegh

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Blue fluorescent proteins (BFPs) offer visualization of protein location and behavior, but often suffer from high autofluorescent background and poor signal discrimination. Through dual-laser excitation of bright and photoinduced dark states, mutations to the residues surrounding the BFP chromophore enable long-wavelength optical modulation of BFP emission.(More)
The fluorescent protein aptly named "Killer Red" (KRed) is capable of killing transfected cells and inactivating fused proteins upon exposure to visible light in the presence of oxygen. We have investigated the source of the bioactive species through a variety of photophysical and photochemical techniques. Our results indicate a Type I (electron transfer(More)
Understanding the photoinduced dynamics of fluorescent proteins is essential for their applications in bioimaging. Despite numerous studies on the ultrafast dynamics, the delayed response of these proteins, which often results in population of kinetically trapped dark states of various origins, is largely unexplored. Here, by using transient absorption(More)
The effect of pH on the spectral and redox properties of model GFP synthetic chromophores (Cros) in a universal buffer system was investigated. The Cro hydroxy-derivatives demonstrated a Nernst-type electrochemical dependence of the anodic potential within the pH 2-8 range. Analogous studies on various fluorescent proteins were unsuccessful.
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