Detail výsledku
FireProt 2.0: Web-based Platform for the Fully-Automated Design of Thermostable Proteins
Ježík Andrej, Bc.
Borko Simeon, Ing.
Damborský Jiří, prof. Mgr., Dr., UMEL (FEKT)
Bednář David, FIT (FIT)
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
@misc{BUT185175,
author="Miloš {Musil} and Andrej {Ježík} and Simeon {Borko} and Jiří {Damborský} and David {Bednář}",
title="FireProt 2.0: Web-based Platform for the Fully-Automated Design of Thermostable Proteins",
year="2023",
pages="1",
address="Lyon"
}