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• W2546670963 abstract "Near-infrared fluorescent proteins (NIR FPs) engineered from bacterial phytochromes and their mutants with different location of Cys residues, which able to bind a biliverdin chromophore, or without these Cys residues were studied using intrinsic tryptophan fluorescence, NIR fluorescence and circular dichroism. It was shown that a covalent binding of the biliverdin chromophore to a Cys residue via thioether group substantially stabilizes the spatial structure of NIR FPs. The stability of the protein structure and the chromophore association strength strongly depends on the location of Cys residues and decreases in the following order: a protein with Cys residues in both domains, a protein with Cys in PAS domains, and a protein with Cys in GAF domains. NIR FPs without Cys residues capable to covalently attach biliverdin have the lowest stability, comparable to NIR FP apoforms." @default.
• W2546670963 created "2016-11-11" @default.
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• W2546670963 date "2017-07-01" @default.
• W2546670963 modified "2023-09-27" @default.
• W2546670963 title "Stabilization of structure in near-infrared fluorescent proteins by binding of biliverdin chromophore" @default.
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• W2546670963 doi "https://doi.org/10.1016/j.molstruc.2016.10.095" @default.
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