FireProt 2.0: Web-based Platform for the Fully-Automated Design of Thermostable Proteins

prezentace, poster

angličtina

Thermostable proteins find their use in numerous biomedical and biotechnological applications. However, the computational design of stable proteins is an uneasy task that usually results in a set of single-point mutations with a limited effect on protein stability.

FireProt 2.0 builds on top of the previously published FireProt-web, retaining all of the original functionality and expanding it with several new strategies and quality-of-life improvements. Compared to its predecessor, new FireProt server provides users with additional multiple-point designs constructed using a novel approach based on the Bron-Kerbosch algorithm minimizing the antagonistic effect between the individual mutations.

Furthermore, it is possible to limit the FireProt calculation to a set of user-defined mutations, run a saturation mutagenesis of the whole protein, or select mutations based on the bfactor analysis. Potentially stabilizing mutations predicted from the sequences constructed by ancestral sequence reconstruction are now available as a second evolution-based strategy. FireProt also integrates the AlphaFold database and the homology modeling utilizing ProMod3. Finally, the second version is significantly faster compared to its predecessor reducing the calculation time from over a week to 1-2 days of time and reworked user interface broadens the availability of the tool even to the users with older hardware.

protein engineering, thermostable proteins, multiple-point mutant prediction, protein stability

MUSIL, M.; JEŽÍK, A.; BORKO, S.; DAMBORSKÝ, J.; BEDNÁŘ, D.

23. 7. 2023

Lyon

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