R 2017

FireProt 1.0

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

Základní údaje

Originální název

FireProt 1.0

Autoři

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

Vydání

2017

Další údaje

Jazyk

angličtina

Typ výsledku

Software

Obor

10201 Computer sciences, information science, bioinformatics

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Odkazy

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/17:00100360

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

protein engineering; thermostable proteins; multiple-point mutant prediction; protein stability

Technické parametry

licenční smlouva není uzavřená

Štítky

Změněno: 14. 3. 2018 11:06, prof. Mgr. Jiří Damborský, Dr.

Anotace

V originále

FireProt is a web server for an automated design of thermostable mutants. The design of thermostable mutants is based on the integration of structural and evolutionary information obtained from several bioinformatics databases and computational tools. FireProt strategy combines energy- and evolution-based approaches together with several filters that accelerate the calculation by omitting potentially deleterious mutations. Within its workflow, FireProt integrates 16 computational tools, utilizing both sequence and structural information in the process. FireProt web server provides users with a one-stop-shop solution for the design of thermostable proteins, constructed by three distinct strategies: (i) evolution-based approach, utilizing back-to-consensus analysis; (ii) energy-based approach, using conservation, correlation and energy information and (iii) combined approach. Furthermore, the server allows users to include user-defined mutations into the constructed thermostable protein and generate corresponding sequences in the FASTA format. The results are visualized in the web browser in an intuitive and comprehensive way, allowing users to directly analyze the designed proteins.