About: Thermostability of Multidomain Proteins: Elongation Factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and Their Chimeric Forms.

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Thermostability of Multidomain Proteins: Elongation Factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and Their Chimeric Forms. Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Recombinant mesophilic E. coli (Ec) and thermophilic B. stearothermophilus (Bst) elongation factors EF-Tu, their isolated G-domains and six chimeric EF-Tus composed of domains of either EF-Tu were prepared and their GDP/GTP binding activities and thermostability characterized. BstEF-Tu and BstG-domain bound GDP and GTP with affinities in nanomolar and submicromolar ranges, respectively, fully comparable with those of EcEF-Tu. In contrast, the EcG-domain bound the nucleotides with much lower, micromolar affinities. The exchange of domains 2, 3 had essentially no effect on the GDP binding activity, all complexes of chimeric EF-Tus with GDP retained Kds in the nanomolar range. The final thermostability level of either EF-Tu was the result of a cooperative interaction between the G-domains and domains 2+3. The G-domains set up a basic level of the thermostability, which was about 20 0C higher with the BstG-domain than with the EcG-domain. Recombinant mesophilic E. coli (Ec) and thermophilic B. stearothermophilus (Bst) elongation factors EF-Tu, their isolated G-domains and six chimeric EF-Tus composed of domains of either EF-Tu were prepared and their GDP/GTP binding activities and thermostability characterized. BstEF-Tu and BstG-domain bound GDP and GTP with affinities in nanomolar and submicromolar ranges, respectively, fully comparable with those of EcEF-Tu. In contrast, the EcG-domain bound the nucleotides with much lower, micromolar affinities. The exchange of domains 2, 3 had essentially no effect on the GDP binding activity, all complexes of chimeric EF-Tus with GDP retained Kds in the nanomolar range. The final thermostability level of either EF-Tu was the result of a cooperative interaction between the G-domains and domains 2+3. The G-domains set up a basic level of the thermostability, which was about 20 0C higher with the BstG-domain than with the EcG-domain. (en)
Title	Thermostability of Multidomain Proteins: Elongation Factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and Their Chimeric Forms. Thermostability of Multidomain Proteins: Elongation Factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and Their Chimeric Forms. (en)
skos:prefLabel	Thermostability of Multidomain Proteins: Elongation Factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and Their Chimeric Forms. Thermostability of Multidomain Proteins: Elongation Factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and Their Chimeric Forms. (en)
skos:notation	RIV/68378050:_____/04:23033143!RIV/2004/GA0/A23004/N
http://linked.open.../vavai/riv/strany	89;99
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(GA204/98/0863), P(GA303/02/0689), P(IPP1050128), Z(AV0Z4055905), Z(AV0Z5052915)
http://linked.open...iv/cisloPeriodika	1
http://linked.open...vai/riv/dodaniDat	2004
http://linked.open...aciTvurceVysledku	Hůlková, Marta Šanderová, Hana Jonák, Jiří
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Ústav molekulární genetiky AV ČR, v. v. i.
http://linked.open...dnocenehoVysledku	590263
http://linked.open...ai/riv/idVysledku	RIV/68378050:_____/04:23033143
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	elongation factor EF-Tu, thermostability, chimeric protein (en)
http://linked.open.../riv/klicoveSlovo	elongation factor EF-Tu thermostability chimeric protein
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[D7AEDE6E9789]
http://linked.open...i/riv/nazevZdroje	Protein Science
http://linked.open...in/vavai/riv/obor	EB
http://linked.open...ichTvurcuVysledku	3 (xsd:int)
http://linked.open...cetTvurcuVysledku	5 (xsd:int)
http://linked.open...ocetUcastnikuAkce	0 (xsd:int)
http://linked.open...nichUcastnikuAkce	0 (xsd:int)
http://linked.open...vavai/riv/projekt	Thermostability of proteins - mutagenesis of elongation factor Tu from Bacillus stearothermophilus Artificial Evolution of Thermostable Elongation Factor Tu Dynamics of processes in living and inanimate matter
http://linked.open...UplatneniVysledku	2004
http://linked.open...v/svazekPeriodika	13
http://linked.open...iv/tvurceVysledku	Maloň, Petr Šanderová, Hana Jonák, Jiří Hůlková, Marta Kepková, M.
http://linked.open...n/vavai/riv/zamer	Chemical principles of selected biological phenomena in medicine and ecology Regulace a signální cesty uplatňující se v genové expresi, imunitě, onkogenezi, replikaci virů, tvorbě buněčných struktur, chování buněk, vývoji a oplození
issn	0961-8368
number of pages	11 (xsd:int)

Faceted Search & Find service v1.16.118 as of Jun 21 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 58 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software