TNP-ATP binding a protein

TNP-ATP is a fluorescent analog of ATP, or adenosine triphosphate.[1]

TNP refers to the chemical compound 2,4,6-trinitrophenol, also known as Picric acid.[2]

TNP is excited at a wavelength of 408 and 470 nm, and fluoresces in the 530-560 nm range. When TNP-ATP is in solution but not bound to a protein, this emission is very weak. However, once TNP-ATP binds to a protein, the TNP fluorescence is markedly enhanced. Thus, with enhanced fluorescence, it can be seen whether or not a protein binds to ATP.[3][4][5][6]


  1. ^ Hiratsuka, Toshiaki (February 2003). "Fluorescent and colored trinitrophenylated analogs of ATP and GTP". European Journal of Biochemistry. 
  2. ^ Deng, Xiang, Xiaomei Huang, and Di Wu. "Förster Resonance-energy-transfer Detection of 2,4,6-trinitrophenol Using Copper Nanoclusters." Anal Bioanal Chem Analytical and Bioanalytical Chemistry 407.16 (2015): 4607-613. Web.
  3. ^ Fujita, Suguru, Tomoko Nawata, and Kazuhiro Yamada. "Fluorescence Changes of a Label Attached near the Myosin Active Site on Nucleotide Binding in Rat Skeletal Muscle Fibres." The Journal of Physiology 515.3 (1999):869-80. Web.
  4. ^ Guarnieri, Michael T., Brian S. J. Blagg, and Rui Zhao. "A High-Throughput TNP-ATP Displacement Assay for Screening Inhibitors of ATP-Binding in Bacterial Histidine Kinases." ASSAY and Drug Development Technologies 9.2 (2011): 174-83. Web.
  5. ^ Hiratsuka, T., and K. Uchida. "Preparation and Properties of 2′(or 3′)-O-(2,4,6-trinitrophenyl) Adenosine 5′-triphosphate, an Analog of Adenosine Triphosphate." Biochimica Et Biophysica Acta (BBA) - General Subjects 320.3 (1973): 635-47. Web.
  6. ^ Stewart, Richard C., Ricaele Vanbruggen, Dolph D. Ellefson, and Alan J. Wolfe. "TNP-ATP and TNP-ADP as Probes of the Nucleotide Binding Site of CheA, the Histidine Protein Kinase in the Chemotaxis Signal Transduction Pathway of Escherichia Coli †." Biochemistry 37.35 (1998): 12269-2279. Web.