@article{
 title = {Improved Stability and Half-Life of Fluorinated Phosphotriesterase Using Rosetta},
 type = {article},
 year = {2014},
 identifiers = {[object Object]},
 keywords = {amino acids; biosynthesis; computational design; h},
 pages = {1761-1764},
 volume = {15},
 month = {8},
 publisher = {WILEY-V C H VERLAG GMBH},
 city = {BOSCHSTRASSE 12, D-69469 WEINHEIM, GERMANY},
 id = {9004c548-efca-3d10-9341-1b14bf9e68b4},
 created = {2015-12-14T19:51:24.000Z},
 file_attached = {false},
 profile_id = {3187ec9d-0fcc-3ba2-91e0-3075df9b18c3},
 group_id = {d75e47fd-ff52-3a4b-bf1e-6ebc7e454352},
 last_modified = {2017-03-14T12:30:08.401Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {true},
 hidden = {false},
 citation_key = {ISI:000340506200010},
 source_type = {article},
 user_context = {Article},
 private_publication = {false},
 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.},
 bibtype = {article},
 author = {Yang, Ching-Yao and Renfrew, P Douglas and Olsen, Andrew J and Zhang, Michelle and Yuvienco, Carlo and Bonneau, Richard and Montclare, Jin Kim},
 journal = {CHEMBIOCHEM},
 number = {12, SI}
}

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