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NanoFAST: structure-based design of a small fluorogen-activating protein with only 98 amino acids
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 str...
Autores principales: | , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8132994/ https://www.ncbi.nlm.nih.gov/pubmed/34040747 http://dx.doi.org/10.1039/d1sc01454d |
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author | Mineev, Konstantin S. Goncharuk, Sergey A. Goncharuk, Marina V. Povarova, Natalia V. Sokolov, Anatolii I. Baleeva, Nadezhda S. Smirnov, Alexander Yu. Myasnyanko, Ivan N. Ruchkin, Dmitry A. Bukhdruker, Sergey Remeeva, Alina Mishin, Alexey Borshchevskiy, Valentin Gordeliy, Valentin Arseniev, Alexander S. Gorbachev, Dmitriy A. Gavrikov, Alexey S. Mishin, Alexander S. Baranov, Mikhail S. |
author_facet | Mineev, Konstantin S. Goncharuk, Sergey A. Goncharuk, Marina V. Povarova, Natalia V. Sokolov, Anatolii I. Baleeva, Nadezhda S. Smirnov, Alexander Yu. Myasnyanko, Ivan N. Ruchkin, Dmitry A. Bukhdruker, Sergey Remeeva, Alina Mishin, Alexey Borshchevskiy, Valentin Gordeliy, Valentin Arseniev, Alexander S. Gorbachev, Dmitriy A. Gavrikov, Alexey S. Mishin, Alexander S. Baranov, Mikhail S. |
author_sort | Mineev, Konstantin S. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-8132994 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | The Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-81329942021-05-25 NanoFAST: structure-based design of a small fluorogen-activating protein with only 98 amino acids Mineev, Konstantin S. Goncharuk, Sergey A. Goncharuk, Marina V. Povarova, Natalia V. Sokolov, Anatolii I. Baleeva, Nadezhda S. Smirnov, Alexander Yu. Myasnyanko, Ivan N. Ruchkin, Dmitry A. Bukhdruker, Sergey Remeeva, Alina Mishin, Alexey Borshchevskiy, Valentin Gordeliy, Valentin Arseniev, Alexander S. Gorbachev, Dmitriy A. Gavrikov, Alexey S. Mishin, Alexander S. Baranov, Mikhail S. Chem Sci Chemistry 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. The Royal Society of Chemistry 2021-04-08 /pmc/articles/PMC8132994/ /pubmed/34040747 http://dx.doi.org/10.1039/d1sc01454d Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/ |
spellingShingle | Chemistry Mineev, Konstantin S. Goncharuk, Sergey A. Goncharuk, Marina V. Povarova, Natalia V. Sokolov, Anatolii I. Baleeva, Nadezhda S. Smirnov, Alexander Yu. Myasnyanko, Ivan N. Ruchkin, Dmitry A. Bukhdruker, Sergey Remeeva, Alina Mishin, Alexey Borshchevskiy, Valentin Gordeliy, Valentin Arseniev, Alexander S. Gorbachev, Dmitriy A. Gavrikov, Alexey S. Mishin, Alexander S. Baranov, Mikhail S. NanoFAST: structure-based design of a small fluorogen-activating protein with only 98 amino acids |
title | NanoFAST: structure-based design of a small fluorogen-activating protein with only 98 amino acids |
title_full | NanoFAST: structure-based design of a small fluorogen-activating protein with only 98 amino acids |
title_fullStr | NanoFAST: structure-based design of a small fluorogen-activating protein with only 98 amino acids |
title_full_unstemmed | NanoFAST: structure-based design of a small fluorogen-activating protein with only 98 amino acids |
title_short | NanoFAST: structure-based design of a small fluorogen-activating protein with only 98 amino acids |
title_sort | nanofast: structure-based design of a small fluorogen-activating protein with only 98 amino acids |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8132994/ https://www.ncbi.nlm.nih.gov/pubmed/34040747 http://dx.doi.org/10.1039/d1sc01454d |
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