Detailed Information on Publication Record
2017
FireProt: Web Server for Automated Design of Thermostable Proteins
MUSIL, Miloš, Jan ŠTOURAČ, Jaroslav BENDL, Jan BREZOVSKÝ, Zbyněk PROKOP et. al.Basic information
Original name
FireProt: Web Server for Automated Design of Thermostable Proteins
Authors
MUSIL, Miloš (203 Czech Republic, belonging to the institution), Jan ŠTOURAČ (203 Czech Republic, belonging to the institution), Jaroslav BENDL (203 Czech Republic, belonging to the institution), Jan BREZOVSKÝ (203 Czech Republic, belonging to the institution), Zbyněk PROKOP (203 Czech Republic, belonging to the institution), Jaroslav ZENDULKA (203 Czech Republic), Tomáš MARTÍNEK (203 Czech Republic, belonging to the institution), David BEDNÁŘ (203 Czech Republic, belonging to the institution) and Jiří DAMBORSKÝ (203 Czech Republic, guarantor, belonging to the institution)
Edition
Nucleic Acids Research, Oxford, Oxford University Press, 2017, 0305-1048
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10608 Biochemistry and molecular biology
Country of publisher
United Kingdom of Great Britain and Northern Ireland
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 11.561
RIV identification code
RIV/00216224:14310/17:00095410
Organization unit
Faculty of Science
UT WoS
000404427000059
Keywords in English
MULTIPLE SEQUENCE ALIGNMENTS; CORRELATED MUTATIONS; STABILITY CHANGES; EVOLUTIONARY CONSERVATION; HALOALKANE DEHALOGENASE; STATISTICAL POTENTIALS; PATHWAYS; BIOCATALYSTS; PREDICTION; FAMILIES
Změněno: 3/4/2018 16:05, Ing. Nicole Zrilić
Abstract
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.
Links
GA16-06096S, research and development project |
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LO1214, research and development project |
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