Publication Details
FireProt: web server for automated design of thermostable proteins
Štourač Jan
Bendl Jaroslav, Ing., Ph.D.
Brezovský Jan
Prokop Zbyněk
Zendulka Jaroslav, doc. Ing., CSc. (UIFS)
Martínek Tomáš, doc. Ing., Ph.D. (DCSY)
Bednář David
Damborský Jiří, prof. Mgr., Dr. (UMEL)
mutations, protein engineering, mutant proteins, protein stability, thermostable
proteins
There is a continuous interest in increasing proteins stability to enhance their
usability in numerous biomedical and biotechnological applications. A number of
in silico tools for the prediction of the effect of mutations on protein
stability have been developed recently. However, only single-point mutations with
a small effect on protein stability are typically predicted with the existing
tools and have to be followed by laborious protein expression, purification, and
characterization. Here, we present FireProt, a web server for the automated
design of multiplepoint thermostable mutant proteins that combines structural and
evolutionary information in its calculation core. FireProt utilizes sixteen tools
and three protein engineering strategies for making reliable protein designs. The
server is complemented with interactive, easy-to-use interface that allows users
to directly analyze and optionally modify designed thermostable mutants. FireProt
is freely available at http://loschmidt.chemi.muni.cz/fireprot.
@article{BUT144434,
author="Miloš {Musil} and Jan {Štourač} and Jaroslav {Bendl} and Jan {Brezovský} and Zbyněk {Prokop} and Jaroslav {Zendulka} and Tomáš {Martínek} and David {Bednář} and Jiří {Damborský}",
title="FireProt: web server for automated design of thermostable proteins",
journal="Nucleic Acids Research",
year="2017",
volume="45",
number="1",
pages="393--399",
doi="10.1093/nar/gkx285",
issn="1362-4962",
url="https://doi.org/10.1093/nar/gkx285"
}