An activity-independent selection system of thermostable protein variants.
basic_science · Level V
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Abstract
We describe an activity-independent method for the selection of thermostable mutants of any protein. It is based on a fusion construct comprising the protein of interest and a thermostable antibiotic resistance reporter, in such a way that thermostable mutants provide increased resistance in a thermophile. We isolated thermostable mutants of three human interferons and of two enzymes to demonstrate the applicability of the system.
Medical subject headings
- Hot Temperature
- Protein Engineering
- Proteins