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10.1038/nmeth.3891

http://scihub22266oqcxt.onion/10.1038/nmeth.3891
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C4927352!4927352!27240257
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suck abstract from ncbi


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pmid27240257      Nat+Methods 2016 ; 13 (7): 557-62
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  • Quantitative Assessment of Fluorescent Proteins #MMPMID27240257
  • Cranfill PJ; Sell BR; Baird MA; Allen JR; Lavagnino Z; de Gruiter HM; Kremers GJ; Davidson MW; Ustione A; Piston DW
  • Nat Methods 2016[Jul]; 13 (7): 557-62 PMID27240257show ga
  • The advent of fluorescent proteins (FP) for genetic labeling of molecules and cells has revolutionized fluorescence microscopy. Genetic manipulations have created a vast array of bright and stable FPs spanning the blue to red spectral regions. Common to autofluorescent FPs is their tight ?-barrel structure, which provides the rigidity and chemical environment needed for effectual fluorescence. Despite the common structure, each FP has its own unique photophysical properties. Thus, there is no single ?best? fluorescent protein for every circumstance, and each FP has advantages and disadvantages. To guide decisions about which FP is right for any given application, we have characterized quantitatively over 40 different FPs for their brightness, photostability, pH stability, and monomeric properties, which permits easy apples-to-apples comparisons between these FPs. We report the values for all of the FPs measured, but focus the discussion on the more popular and/or best performing FPs in each spectral region.
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