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- W2307372020 abstract "The interconversion of nucleoside triphosphate (NTP) and diphosphate occurs in some of the most -important cellular reactions. It is catalyzed by diverse classes of enzymes, such as nucleoside triphosphatases, kinases, and ATP synthases. Triphosphatases include helicases, myosins, and G-proteins, as well as many other energy-transducing enzymes. The transfer of phosphate by kinases is involved in many metabolic pathways and in control of enzyme activity through protein phosphorylation. To understand the processes catalyzed by these enzymes, it is important to measure the kinetics of individual elementary steps and conformation changes. Fluorescent nucleotides can directly report on the binding and release steps, and conformational changes associated with these processes. In single-molecule studies, fluorescent nucleotides can allow their role to be explored by following precisely the temporal and spatial changes in the bound nucleotide. Here, the selection of fluorophores and nucleotide modifications are discussed and methods are described to prepare ATP analogs with examples of two alternate fluorophores, diethylaminocoumarin and Cy3." @default.
- W2307372020 created "2016-06-24" @default.
- W2307372020 creator A5051163780 @default.
- W2307372020 creator A5078281981 @default.
- W2307372020 date "2011-01-01" @default.
- W2307372020 modified "2023-10-12" @default.
- W2307372020 title "Fluorescent Nucleoside Triphosphates for Single-Molecule Enzymology" @default.
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- W2307372020 doi "https://doi.org/10.1007/978-1-61779-261-8_11" @default.
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