Abstract
Recently we demonstrated that incorporating p-fluorophenylalanine (pFF) into phosphotriesterase dramatically improved folding, thereby leading to enhanced stability and function at elevated temperatures. To further improve the stability of the fluorinated enzyme, Rosetta was used to identify multiple potential stabilizing mutations. One such variant, pFF-F104A, exhibited enhanced activity at elevated temperature and maintained activity over many days in solution at room temperature. Rock solid: To improve stability, Rosetta was used to identify the fluorinated phosphotriesterase variant, pFF-F104A. Surprisingly, pFF-F104A not only exhibited enhanced activity at elevated temperatures but also maintained activity over several days.
Original language | English (US) |
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Pages (from-to) | 1761-1764 |
Number of pages | 4 |
Journal | ChemBioChem |
Volume | 15 |
Issue number | 12 |
DOIs | |
State | Published - Aug 18 2014 |
Keywords
- amino acids
- biosynthesis
- computational design
- half-life
- noncanonical amino acids
- stability
ASJC Scopus subject areas
- Biochemistry
- Molecular Medicine
- Molecular Biology
- Organic Chemistry