About: Thermostability of Multidomain Proteins: Properties of Chimaeric Elongation Factors EF-Tu Composed of Domains of Mesophilic-Escherichia coli EF-Tu and Thermophilic-Bacillus stearothermophilus EF-Tu.

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About: Thermostability of Multidomain Proteins: Properties of Chimaeric Elongation Factors EF-Tu Composed of Domains of Mesophilic-Escherichia coli EF-Tu and Thermophilic-Bacillus stearothermophilus EF-Tu. Goto Sponge NotDistinct Permalink

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	The EF-Tu proteins from E. coli and B. stearothermophilus were examined by the chimaerization approach to evaluate the contribution of the domains to the thermostability of these proteins. Molecules of EF-Tus were genetically dissected into three corresponding domains and the domains combined to form chimaeric EF-Tu proteins. The resulting six recombinant mesophile/thermophile chimaeric EF-Tus, together with the recombinant E. coli and B. stearothermophilus EF-Tus and isolated G-domains, were characterized with regard to GDP and GTP binding activity, intrinsic GTPase activity and thermostability. The thermostability was measured both as the maintenance, at increasing temperatures, of a defined functional state by the ability to bind GDP and GTP, and to hydrolyze GTP and, independently, using CD spectroscopy, as the maintenance of the alfa-helix content. The EF-Tu proteins from E. coli and B. stearothermophilus were examined by the chimaerization approach to evaluate the contribution of the domains to the thermostability of these proteins. Molecules of EF-Tus were genetically dissected into three corresponding domains and the domains combined to form chimaeric EF-Tu proteins. The resulting six recombinant mesophile/thermophile chimaeric EF-Tus, together with the recombinant E. coli and B. stearothermophilus EF-Tus and isolated G-domains, were characterized with regard to GDP and GTP binding activity, intrinsic GTPase activity and thermostability. The thermostability was measured both as the maintenance, at increasing temperatures, of a defined functional state by the ability to bind GDP and GTP, and to hydrolyze GTP and, independently, using CD spectroscopy, as the maintenance of the alfa-helix content. (en)
Title	Thermostability of Multidomain Proteins: Properties of Chimaeric Elongation Factors EF-Tu Composed of Domains of Mesophilic-Escherichia coli EF-Tu and Thermophilic-Bacillus stearothermophilus EF-Tu. Thermostability of Multidomain Proteins: Properties of Chimaeric Elongation Factors EF-Tu Composed of Domains of Mesophilic-Escherichia coli EF-Tu and Thermophilic-Bacillus stearothermophilus EF-Tu. (en)
skos:prefLabel	Thermostability of Multidomain Proteins: Properties of Chimaeric Elongation Factors EF-Tu Composed of Domains of Mesophilic-Escherichia coli EF-Tu and Thermophilic-Bacillus stearothermophilus EF-Tu. Thermostability of Multidomain Proteins: Properties of Chimaeric Elongation Factors EF-Tu Composed of Domains of Mesophilic-Escherichia coli EF-Tu and Thermophilic-Bacillus stearothermophilus EF-Tu. (en)
skos:notation	RIV/68378050:_____/03:23033142!RIV/2004/GA0/A23004/N
http://linked.open.../vavai/riv/strany	308;309
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(GA204/98/0863), P(GA303/02/0689), Z(AV0Z4055905), Z(AV0Z5052915)
http://linked.open...iv/cisloPeriodika	5
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	630957
http://linked.open...ai/riv/idVysledku	RIV/68378050:_____/03:23033142
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	CZ - Česká republika
http://linked.open...ontrolniKodProRIV	[6775B449DC53]
http://linked.open...i/riv/nazevZdroje	Chemické listy
http://linked.open...in/vavai/riv/obor	EB
http://linked.open...ichTvurcuVysledku	3 (xsd:int)
http://linked.open...cetTvurcuVysledku	4 (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
http://linked.open...UplatneniVysledku	2003
http://linked.open...v/svazekPeriodika	97
http://linked.open...iv/tvurceVysledku	Maloň, Petr Šanderová, Hana Jonák, Jiří Hůlková, Marta
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	0009-2770
number of pages	2 (xsd:int)

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