Positional effects of monofluorinated phenylalanines on histone acetyltransferase stability and activity |
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Authors: | Natalya Voloshchuk Anita Y. Zhu David Snydacker Jin Kim Montclare |
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Affiliation: | aDepartment of Chemical and Biological Sciences, Polytechnic Institute of New York University, Brooklyn, NY 11201, USA;bDepartment of Biochemistry, SUNY-Downstate Medical Center, Brooklyn, NY 11203, USA |
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Abstract: | To explore the impact of global incorporation of fluorinated aromatic amino acids on protein function, we investigated the effects of three monofluorinated phenylalanine analogs para-fluorophenylalanine (pFF), meta-fluorophenylalanine (mFF), and ortho-fluorophenylalanine (oFF) on the stability and enzymatic activity of the histone acetyltransferase (HAT), tGCN5. We selected this set of fluorinated amino acids because they bear the same size and overall polarity but alter in side chain shape and dipole direction. Our experiments showed that among three fluorinated amino acids, the global incorporation of pFF affords the smallest perturbation to the structure and function of tGCN5. |
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Keywords: | Fluorinated amino acids Histone acetyltransferase Activity Stability Protein design |
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