About: Thermostability of multidomain proteins: chimeric mesophilic/thermophilic elongation factors EF-Tu     Goto   Sponge   NotDistinct   Permalink

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  • EF-Tus are abundant three-domain GTPases involved in mRNA translation in all known microorganisms. Their domain 1 has a GTPase activity, binds GDP and GTP and is called the G-domain. The high homology of various EF-Tus predetermines them for the elucidation of structural features of adaptation to different living conditions. The EF-Tu from moderately thermostable G+ bacterium Bacillus stearothermophilus (Bst), growing around 60C, was chosen to determine the contribution of individual domains to its thermostability to learn what makes it more thermostable than EF-Tu from mesophilic Escherichia coli (Ec). For this purpose chimeric forms of EF-Tu composed of mesophilic and thermophilic domains and isolated G-domains were prepared and their functional parameters and thermostability were characterized. The final thermostability of either EF-Tu was found to be the result of a cooperative interaction between the G-domain and domains 2+3. The G-domain set up the ôbasicö level of the thermos...
  • EF-Tus are abundant three-domain GTPases involved in mRNA translation in all known microorganisms. Their domain 1 has a GTPase activity, binds GDP and GTP and is called the G-domain. The high homology of various EF-Tus predetermines them for the elucidation of structural features of adaptation to different living conditions. The EF-Tu from moderately thermostable G+ bacterium Bacillus stearothermophilus (Bst), growing around 60C, was chosen to determine the contribution of individual domains to its thermostability to learn what makes it more thermostable than EF-Tu from mesophilic Escherichia coli (Ec). For this purpose chimeric forms of EF-Tu composed of mesophilic and thermophilic domains and isolated G-domains were prepared and their functional parameters and thermostability were characterized. The final thermostability of either EF-Tu was found to be the result of a cooperative interaction between the G-domain and domains 2+3. The G-domain set up the ôbasicö level of the thermos... (en)
  • Faktory EF-Tu jsou hojně se vyskytující třídoménové GTPázy podílející se na translaci mRNA ve všech známých mikroorganismech. Jejich doména 1 má GTPázovou aktivitu, váže GDP a GTP a nazývá se doména G. Vysoká homologie různých EF-Tu je předurčuje k objasnění strukturních vlastností adaptace na různé životní podmínky. EF-Tu z mírně termostabilní G+ bakterie Bacillus stearothermophilus (Bst), rostoucí při cca 60°C, byla vybrána k určení podílu jednotlivých domén na její termostabilitě, abychom zjistili, co způsobuje jeho vyšší termostabilitu ve srovnání s EF-Tu z mezofilní Escherichia coli (Ec). Za tímto účelem byly připraveny chimerické formy EF-Tu složené z mezofilních a termofilních domén a izolovaných domén G a byly charakterizovány jejich funkční parametry a termostabilita. Bylo zjištěno, že konečná termostabilita obou EF-Tu je výsledkem kooperativní interakce mezi doménou G a doménami 2+3. Doména G nastavila %22základní%22 hladinu termostability, která byla asi o 20°C vyšší u domény... (cs)
Title
  • Thermostability of multidomain proteins: chimeric mesophilic/thermophilic elongation factors EF-Tu
  • ??? (cs)
  • Thermostability of multidomain proteins: chimeric mesophilic/thermophilic elongation factors EF-Tu (en)
skos:prefLabel
  • Thermostability of multidomain proteins: chimeric mesophilic/thermophilic elongation factors EF-Tu
  • ??? (cs)
  • Thermostability of multidomain proteins: chimeric mesophilic/thermophilic elongation factors EF-Tu (en)
skos:notation
  • RIV/68378050:_____/04:00105330!RIV/2005/AV0/A23005/N
http://linked.open.../vavai/riv/strany
  • 7
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(GA303/02/0689), Z(AV0Z5052915)
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 590261
http://linked.open...ai/riv/idVysledku
  • RIV/68378050:_____/04:00105330
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • thermostability; EF-Tu; chimeric protein (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...ontrolniKodProRIV
  • [38772F748510]
http://linked.open...v/mistoKonaniAkce
  • Varšava
http://linked.open...i/riv/mistoVydani
  • Varšava
http://linked.open...i/riv/nazevZdroje
  • FEBS Forum For Young Scientists, Abstract book
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...iv/tvurceVysledku
  • Maloň, Petr
  • Šanderová, Hana
  • Jonák, Jiří
  • Hůlková, Marta
http://linked.open...vavai/riv/typAkce
http://linked.open.../riv/zahajeniAkce
http://linked.open...n/vavai/riv/zamer
number of pages
http://purl.org/ne...btex#hasPublisher
  • FEBS
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