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ČeštinaEnglish

Thermostability of Multidomain Proteins Studied by Domain Swapping between Mesophilic-Escherichia coli and Thermophilic-Bacillus stearothermophilus Elongation Factors EF-Tu.

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F03%3A23033198" target="_blank" >RIV/68378050:_____/03:23033198 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388963:_____/03:23033198

  • Result on the web

    —

  • DOI - Digital Object Identifier

    —

Alternative languages

  • Result language

    angličtina

  • Original language name

    Thermostability of Multidomain Proteins Studied by Domain Swapping between Mesophilic-Escherichia coli and Thermophilic-Bacillus stearothermophilus Elongation Factors EF-Tu.

  • Original language description

    EF-Tu from moderately thermostable G+ bacterium Bacillus stearothermophilus, growing at around 60 0C, was chosen to determine how its overall thermostability is built from the contribution of individual protein domains and what makes this protein more thermostable than EF-Tu from mesophilic Escherichia coli (growing at 37 0C). For this purpose chimaeric forms of EF-Tu composed of domains of the mesophilic and thermophilic EF-Tus were constructed and their activity and thermostability compared with thoseof intact EF-Tus and their isolated G-domains.

  • Czech name

    —

  • Czech description

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Classification

  • Type

    D - Article in proceedings

  • CEP classification

    EB - Genetics and molecular biology

  • OECD FORD branch

    —

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)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2003

  • Confidentiality

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

Data specific for result type

  • Article name in the collection

    Program of The Sixth International Engelhardt Conference on Molecular Biology.

  • ISBN

    —

  • ISSN

    —

  • e-ISSN

    —

  • Number of pages

    1

  • Pages from-to

    4

  • Publisher name

    Engelhardt Institute of Molecular Biology

  • Place of publication

    Moscow

  • Event location

    St. Peterburg - Moscow [RU]

  • Event date

    Jun 29, 2003

  • Type of event by nationality

    WRD - Celosvětová akce

  • UT code for WoS article

    —

Similar results(10)

Thermostability of multidomain proteins: chimeric mesophilic/thermophilic elongation factors EF-TuThermostability of multidomain proteins: chimeric mesophilic/thermophilic elongation factors EF-TuThermostability of Multidomain Proteins: Elongation Factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and Their Chimeric Forms.