What is it about?
Protein expression system is important technology for the production of recombinant proteins such as enzyme, antibody etc. To develop an efficient protein expression system, we designed functional peptide. This paper reports mutation peptides based on the functional peptide via point mutations for more efficient protein expression.
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Why is it important?
Glutamic acid, lysine, leucine, and asparagine in the functional peptide increased protein expression. The expression of the mutated LEA peptide was 1.5 to 2.0 times. In contrast, the serine‐containing mutated peptide has low prptein expression levels. .
Perspectives
These data suggest that the size, structure, and charge of amino acids in the peptide improve the protection and expression of the target protein in E.coli. The amino acid balance in the peptide also plays an important role in the expression of the target protein.
Shinya Ikeno
Kyushu Kogyo Daigaku
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This page is a summary of: Construction and characterization of mutated LEA peptides in Escherichia coli
to develop an efficient protein expression system, Journal of Molecular Recognition, August 2017, Wiley,
DOI: 10.1002/jmr.2658.
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