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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F04%3A23033143" target="_blank" >RIV/68378050:_____/04:23033143 - isvavai.cz</a>

Alternative codes found

RIV/61388963:_____/04:23033143

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: Elongation Factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and Their Chimeric Forms.

Original language 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, micromolaraffinities. 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 cooperativeinteraction 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.

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

2004

Confidentiality

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

Name of the periodical

Protein Science

ISSN

0961-8368

e-ISSN

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Volume of the periodical

13

Issue of the periodical within the volume

1

Country of publishing house

US - UNITED STATES

Number of pages

11

Pages from-to

89-99

UT code for WoS article

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EID of the result in the Scopus database

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