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.

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F03%3A23033142" target="_blank" >RIV/68378050:_____/03:23033142 - isvavai.cz</a>

Alternative codes found

RIV/61388963:_____/03:23033142

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

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.

Original language 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 tohydrolyze GTP and, independently, using CD spectroscopy, as the maintenance of the alfa-helix content.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EB - Genetics and molecular biology

OECD FORD branch

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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)

Publication year

2003

Confidentiality

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

Name of the periodical

Chemické listy

ISSN

0009-2770

e-ISSN

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Volume of the periodical

97

Issue of the periodical within the volume

5

Country of publishing house

CZ - CZECH REPUBLIC

Number of pages

2

Pages from-to

308-309

UT code for WoS article

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EID of the result in the Scopus database

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