FireProt: Web Server for Automated Design of Thermostable Proteins

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Authors

MUSIL Miloš ŠTOURAČ Jan BENDL Jaroslav BREZOVSKÝ Jan PROKOP Zbyněk ZENDULKA Jaroslav MARTÍNEK Tomáš BEDNÁŘ David DAMBORSKÝ Jiří

Year of publication 2017
Type Article in Periodical
Magazine / Source Nucleic Acids Research
MU Faculty or unit

Faculty of Science

Citation
Web https://loschmidt.chemi.muni.cz/peg/publications/fireprot-web-server-for-automated-design-of-thermostable-proteins/
Doi http://dx.doi.org/10.1093/nar/gkx285
Keywords MULTIPLE SEQUENCE ALIGNMENTS; CORRELATED MUTATIONS; STABILITY CHANGES; EVOLUTIONARY CONSERVATION; HALOALKANE DEHALOGENASE; STATISTICAL POTENTIALS; PATHWAYS; BIOCATALYSTS; PREDICTION; FAMILIES
Description 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.
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