Team:Heidelberg/Model test2

Modeling
Lagoon contamination
Improved Part Introduction

ß-Lactamase_E102F

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Circularization Construct
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As a result, we decided to perform a second test for these candidates with higher antibiotic concentrations. The three highest carbenicillin concentrations of the first data set were included and the range was extended to a maximum concentration of 19.2 mg/ml. While several candidates turned out to have a weaker activity than the wildtype protein, five of them showed improved properties. The two best candidates could even grow at 19.2 mg/ml (Fig.: 2). The variants were contained one point mutation each, E102F and M67G. These most benefitial mutations, appear in many of our better candidates as well, which underlines there functionality.
Figure 2: Gowth Behaviour of \(\beta\)-Lactamase Mutants under Elevated Carbenicillin Concentrations
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The outstanding candidate was the E102F mutant, which could even grow at 19.2 mg/ml without affection by the antibiotic. This results in a improvement of at least 100 % in comparison to the wildtype ß-lactamase. This remarkable gain of activity proves, that our software is not only able to recognize protein classes, but also to generate new function.
Figure:
The ß-lactamase_E102F was the outstanding candidate of our deep learning software based mutation screen, which could even grow at 19.2 mg/ml without affection by the antibiotic. This results in a improvement of at least 100 % in comparison to the wildtype ß-lactamase. This remarkable gain of activity proves, that our software is not only able to recognize protein classes, but also to generate new function.

References