Article
Trade-offs between enzyme fitness and solubility illuminated by deep mutational scanning.
Proceedings of the National Academy of Sciences of the United States of America - 28 Feb 2017
Klesmith Justin R, Bacik John-Paul, Wrenbeck Emily E, Michalczyk Ryszard, Whitehead Timothy A
Abstract excerpt
Proteins are marginally stable, and an understanding of the sequence determinants for improved protein solubility is highly desired. For enzymes, it is well known that many mutations that increase protein solubility decrease catalytic activity. These competing effects frustrate efforts to design and engineer stable, active enzymes without laborious high-throughput activity screens. To address the trade-off...
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