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Issue 19, 2021

NanoFAST: structure-based design of a small fluorogen-activating protein with only 98 amino acids

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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.

Graphical abstract: NanoFAST: structure-based design of a small fluorogen-activating protein with only 98 amino acids

Supplementary files

Article information


Submitted
12 Mar 2021
Accepted
08 Apr 2021
First published
08 Apr 2021

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2021,12, 6719-6725
Article type
Edge Article

NanoFAST: structure-based design of a small fluorogen-activating protein with only 98 amino acids

K. S. Mineev, S. A. Goncharuk, M. V. Goncharuk, N. V. Povarova, A. I. Sokolov, N. S. Baleeva, A. Yu. Smirnov, I. N. Myasnyanko, D. A. Ruchkin, S. Bukhdruker, A. Remeeva, A. Mishin, V. Borshchevskiy, V. Gordeliy, A. S. Arseniev, D. A. Gorbachev, A. S. Gavrikov, A. S. Mishin and M. S. Baranov, Chem. Sci., 2021, 12, 6719 DOI: 10.1039/D1SC01454D

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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