Targeted-random mutagenesis of PA-IIL lectin and high-throughput screening of mutant library
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Year of publication | 2014 |
Type | Conference abstract |
MU Faculty or unit | |
Citation | |
Description | PA-IIL lectin from Pseudomonas aeruginosa shows a unique binding mode among bacterial lectins because it binds saccharides through two calcium cations. Its features make this protein a good candidate for tuning its affinity and specificity. Two amino acids responsible for sugar binding were chosen for targeted-random mutagenesis. If this approach is used, it is necessary to utilize high-throughput screening of mutant libraries for identification of mutants with interestingly modified specificity and/or affinity. |
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