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FireProt: Web Server for Automated Design of Thermostable Proteins

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

Rok publikování 2017
Druh Článek v odborném periodiku
Časopis / Zdroj Nucleic Acids Research
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
www 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
Klíčová slova MULTIPLE SEQUENCE ALIGNMENTS; CORRELATED MUTATIONS; STABILITY CHANGES; EVOLUTIONARY CONSERVATION; HALOALKANE DEHALOGENASE; STATISTICAL POTENTIALS; PATHWAYS; BIOCATALYSTS; PREDICTION; FAMILIES
Popis 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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