FireProt: Web Server for Automated Design of Thermostable
Proteins

J 2017

FireProt: Web Server for Automated Design of Thermostable Proteins

MUSIL, Miloš; Jan ŠTOURAČ; Jaroslav BENDL; Jan BREZOVSKÝ; Zbyněk PROKOP et al.

Základní údaje

Originální název

FireProt: Web Server for Automated Design of Thermostable Proteins

Autoři

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

Vydání

Nucleic Acids Research, Oxford, Oxford University Press, 2017, 0305-1048

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 11.561

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/17:00095410

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

MULTIPLE SEQUENCE ALIGNMENTS; CORRELATED MUTATIONS; STABILITY CHANGES; EVOLUTIONARY CONSERVATION; HALOALKANE DEHALOGENASE; STATISTICAL POTENTIALS; PATHWAYS; BIOCATALYSTS; PREDICTION; FAMILIES

Štítky

H20, NZ, rivok

Změněno: 3. 4. 2018 16:05, Ing. Nicole Zrilić

Anotace

V originále

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.

Návaznosti

GA16-06096S, projekt VaV

Název: Objasnění významu dynamických tunelů pro enzymatickou katalýzu: simulace a fluorescenční experimenty

Investor: Grantová agentura ČR, Objasnění významu dynamických tunelů pro enzymatickou katalýzu: simulace a fluorescenční experimenty

LO1214, projekt VaV

Název: Centrum pro výzkum toxických látek v prostředí (Akronym: RECETOX)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Centrum pro výzkum toxických látek v prostředí

Citovat

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://doi.org/10.1093/nar/gkx285.

@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 = {https://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://doi.org/10.1093/nar/gkx285.

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