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- W2070060384 endingPage "686" @default.
- W2070060384 startingPage "686" @default.
- W2070060384 abstract "Fluorescence methods allow one to monitor protein conformational changes, protein–protein associations, and proteolysis in real time, at the single molecule level and in living cells. The information gained in such experiments is a function of the spectroscopic techniques used and the strategic placement of fluorophore labels within the protein structure. There is often a trade-off between size and utility for fluorophores, whereby large size can be disruptive to the protein’s fold or function, but valuable characteristics, such as visible wavelength absorption and emission or brightness, require sizable chromophores. Three major types of fluorophore readouts are commonly used: (1) Förster resonance energy transfer (FRET); (2) photoinduced electron transfer (PET); and (3) environmental sensitivity. This review focuses on those probes small enough to be incorporated into proteins during ribosomal translation, which allows the probes to be placed on the interiors of proteins as they are folded during synthesis. The most broadly useful method for doing so is site-specific unnatural amino acid (UAA) mutagenesis. We discuss the use of UAA probes in applications relying on FRET, PET, and environmental sensitivity. We also briefly review other methods of protein labelling and compare their relative merits to UAA mutagenesis. Finally, we discuss small probes that have thus far been used only in synthetic peptides, but which have unusual value and may be candidates for incorporation using UAA methods." @default.
- W2070060384 created "2016-06-24" @default.
- W2070060384 creator A5028662408 @default.
- W2070060384 creator A5051808023 @default.
- W2070060384 creator A5073238665 @default.
- W2070060384 date "2014-01-01" @default.
- W2070060384 modified "2023-10-07" @default.
- W2070060384 title "Minimalist Approaches to Protein Labelling: Getting the Most Fluorescent Bang for Your Steric Buck" @default.
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