FireProt: web server for automated design of 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...

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Bibliographic Details
Published in:Nucleic acids research 2017-07, Vol.45 (W1), p.W393-W399
Main Authors: Musil, Milos, Stourac, Jan, Bendl, Jaroslav, Brezovsky, Jan, Prokop, Zbynek, Zendulka, Jaroslav, Martinek, Tomas, Bednar, David, Damborsky, Jiri
Format: Article
Language:English
Subjects:
Bacteria - chemistry
Bacteria - enzymology
Databases, Protein
Humans
Hydrolases - chemistry
Hydrolases - genetics
Hydrolases - metabolism
Internet
Models, Molecular
Mutation
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Engineering - methods
Protein Interaction Domains and Motifs
Protein Stability
Structure-Activity Relationship
Thermodynamics
User-Computer Interface
Web Server Issue
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Summary: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 multiple-point 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.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gkx285