J 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

Tags

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
Name: Objasnění významu dynamických tunelů pro enzymatickou katalýzu: simulace a fluorescenční experimenty
Investor: Czech Science Foundation
LO1214, research and development project
Name: Centrum pro výzkum toxických látek v prostředí (Acronym: RECETOX)
Investor: Ministry of Education, Youth and Sports of the CR