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FireProt: web server for automated design of thermostable proteins

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00159816%3A_____%2F17%3A00067126" target="_blank" >RIV/00159816:_____/17:00067126 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216224:14310/17:00095410 RIV/00216305:26230/17:PU126411

  • Result on the web

    <a href="http://dx.doi.org/10.1093/nar/gkx285" target="_blank" >http://dx.doi.org/10.1093/nar/gkx285</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1093/nar/gkx285" target="_blank" >10.1093/nar/gkx285</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    FireProt: web server for automated design of thermostable proteins

  • Original language description

    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 multiple-point 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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2017

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Nucleic Acids Research

  • ISSN

    0305-1048

  • e-ISSN

  • Volume of the periodical

    45

  • Issue of the periodical within the volume

    W1

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    7

  • Pages from-to

    "W393"-"W399"

  • UT code for WoS article

    000404427000059

  • EID of the result in the Scopus database