Urychlení stanovení resonancí uhlíkové kostry WT matrixového proteinu MPMV retroviru

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F04%3A00012891" target="_blank" >RIV/60461373:22330/04:00012891 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

SPEEDING UP OF THE ASSIGNMENT OF BACKBONE RESONANCES OF WILD-TYPE MATRIX PROTEIN FROM M-PMV

Popis výsledku v původním jazyce

Several single-point mutants of Mason-Pfizer monkey virus (M-PMV) matrix protein (MA) are known to cause dramatic changes in the virus life-cycle [1]. We started structural and dynamic studies of these molecules in order to reveal relationships between changed virus behavior and possible changes in spatial structures of the MA mutants. Three-dimensional structure of R55F mutant has recently been solved and compared with that of the wild-type (WT) matrix molecule [2]. A substantial structural change wasidentified. However, the structure of WT MA was published as C-alpha trace only [3], which seems to be insufficient for proper structural comparisons. Therefore, we decided to perform complete structural study on WT MA.Doubly isotopicaly labeled (13C, 15N) protein was prepared using recombinant techniques. Triple-resonance experiments for protein backbone resonance assignments were measured and almost all of the resonances have been unambiguously assigned. We will present our experience

Název v anglickém jazyce

SPEEDING UP OF THE ASSIGNMENT OF BACKBONE RESONANCES OF WILD-TYPE MATRIX PROTEIN FROM M-PMV

Popis výsledku anglicky

Several single-point mutants of Mason-Pfizer monkey virus (M-PMV) matrix protein (MA) are known to cause dramatic changes in the virus life-cycle [1]. We started structural and dynamic studies of these molecules in order to reveal relationships between changed virus behavior and possible changes in spatial structures of the MA mutants. Three-dimensional structure of R55F mutant has recently been solved and compared with that of the wild-type (WT) matrix molecule [2]. A substantial structural change wasidentified. However, the structure of WT MA was published as C-alpha trace only [3], which seems to be insufficient for proper structural comparisons. Therefore, we decided to perform complete structural study on WT MA.Doubly isotopicaly labeled (13C, 15N) protein was prepared using recombinant techniques. Triple-resonance experiments for protein backbone resonance assignments were measured and almost all of the resonances have been unambiguously assigned. We will present our experience

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2004

Kód důvěrnosti údajů

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

Název statě ve sborníku

19thNMR Valtice

ISBN

80-210-3352-5

ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

35

Název nakladatele

Masarykova univerzita Brno

Místo vydání

Brno

Místo konání akce

Valtice

Datum konání akce

19. 4. 2004

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

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