Journal
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
Volume 19, Issue 18, Pages 5449-5451Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2009.07.093
Keywords
Fluorinated amino acids; Histone acetyltransferase; Activity; Stability; Protein design
Categories
Funding
- Othmer Institute for Interdisciplinary Studies
- ACS Division of Fluorine Chemistry
- Wechsler Award for Excellence
- AFOSR
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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. (C) 2009 Elsevier Ltd. All rights reserved.
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