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@ARTICLE{Mineev:904330,
      author       = {Mineev, Konstantin S. and Goncharuk, Sergey A. and
                      Goncharuk, Marina V. and Povarova, Natalia V. and Sokolov,
                      Anatolii I. and Baleeva, Nadezhda S. and Smirnov, Alexander
                      Yu. and Myasnyanko, Ivan N. and Ruchkin, Dmitry A. and
                      Bukhdruker, Sergey and Remeeva, Alina and Mishin, Alexey and
                      Borshchevskiy, Valentin and Gordeliy, Valentin and Arseniev,
                      Alexander S. and Gorbachev, Dmitriy A. and Gavrikov, Alexey
                      S. and Mishin, Alexander S. and Baranov, Mikhail S.},
      title        = {{N}ano{FAST}: structure-based design of a small
                      fluorogen-activating protein with only 98 amino acids},
      journal      = {Chemical science},
      volume       = {12},
      number       = {19},
      issn         = {2041-6520},
      address      = {Cambridge},
      publisher    = {RSC},
      reportid     = {FZJ-2021-05900},
      pages        = {6719 - 6725},
      year         = {2021},
      abstract     = {One of the essential characteristics of any tag used in
                      bioscience and medical applications is its size. The larger
                      the label, the more it may affect the studied object, and
                      the more it may distort its behavior. In this paper, using
                      NMR spectroscopy and X-ray crystallography, we have studied
                      the structure of fluorogen-activating protein FAST both in
                      the apo form and in complex with the fluorogen. We showed
                      that significant change in the protein occurs upon
                      interaction with the ligand. While the protein is completely
                      ordered in the complex, its apo form is characterized by
                      higher mobility and disordering of its N-terminus. We used
                      structural information to design the shortened FAST (which
                      we named nanoFAST) by truncating 26 N-terminal residues.
                      Thus, we created the shortest genetically encoded tag among
                      all known fluorescent and fluorogen-activating proteins,
                      which is composed of only 98 amino acids.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34040747},
      UT           = {WOS:000640983900001},
      doi          = {10.1039/D1SC01454D},
      url          = {https://juser.fz-juelich.de/record/904330},
}