MUSIL, Miloš, Jan ŠTOURAČ, Jaroslav BENDL, Jan BREZOVSKÝ, Zbyněk PROKOP, Jaroslav ZENDULKA, Tomáš MARTÍNEK, David BEDNÁŘ a Jiří DAMBORSKÝ. FireProt: Web Server for Automated Design of Thermostable Proteins. Nucleic Acids Research. Oxford: Oxford University Press, 2017, roč. 45, W1, s. "W393"-"W399", 7 s. ISSN 0305-1048. Dostupné z: https://dx.doi.org/10.1093/nar/gkx285. |
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@article{1403851, author = {Musil, Miloš and Štourač, Jan and Bendl, Jaroslav and Brezovský, Jan and Prokop, Zbyněk and Zendulka, Jaroslav and Martínek, Tomáš and Bednář, David and Damborský, Jiří}, article_location = {Oxford}, article_number = {W1}, 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}, language = {eng}, issn = {0305-1048}, journal = {Nucleic Acids Research}, title = {FireProt: Web Server for Automated Design of Thermostable Proteins}, url = {https://loschmidt.chemi.muni.cz/peg/publications/fireprot-web-server-for-automated-design-of-thermostable-proteins/}, volume = {45}, year = {2017} }
TY - JOUR ID - 1403851 AU - Musil, Miloš - Štourač, Jan - Bendl, Jaroslav - Brezovský, Jan - Prokop, Zbyněk - Zendulka, Jaroslav - Martínek, Tomáš - Bednář, David - Damborský, Jiří PY - 2017 TI - FireProt: Web Server for Automated Design of Thermostable Proteins JF - Nucleic Acids Research VL - 45 IS - W1 SP - "W393"-"W399" EP - "W393"-"W399" PB - Oxford University Press SN - 03051048 KW - MULTIPLE SEQUENCE ALIGNMENTS KW - CORRELATED MUTATIONS KW - STABILITY CHANGES KW - EVOLUTIONARY CONSERVATION KW - HALOALKANE DEHALOGENASE KW - STATISTICAL POTENTIALS KW - PATHWAYS KW - BIOCATALYSTS KW - PREDICTION KW - FAMILIES UR - https://loschmidt.chemi.muni.cz/peg/publications/fireprot-web-server-for-automated-design-of-thermostable-proteins/ N2 - 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. ER -
MUSIL, Miloš, Jan ŠTOURAČ, Jaroslav BENDL, Jan BREZOVSKÝ, Zbyněk PROKOP, Jaroslav ZENDULKA, Tomáš MARTÍNEK, David BEDNÁŘ a Jiří DAMBORSKÝ. FireProt: Web Server for Automated Design of Thermostable Proteins. \textit{Nucleic Acids Research}. Oxford: Oxford University Press, 2017, roč.~45, W1, s.~''W393''-''W399'', 7 s. ISSN~0305-1048. Dostupné z: https://dx.doi.org/10.1093/nar/gkx285.
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