The combination of hydrogen/deuterium exchange or chemical cross-linking techniques with mass spectrometry: Mapping of human 14-3-3 zeta homodimer interface

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F12%3A10123293" target="_blank" >RIV/00216208:11310/12:10123293 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/67985823:_____/12:00388476 RIV/61388971:_____/12:00388476

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.jsb.2012.04.016" target="_blank" >http://dx.doi.org/10.1016/j.jsb.2012.04.016</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jsb.2012.04.016" target="_blank" >10.1016/j.jsb.2012.04.016</a>

Jazyk výsledku

angličtina

Název v původním jazyce

The combination of hydrogen/deuterium exchange or chemical cross-linking techniques with mass spectrometry: Mapping of human 14-3-3 zeta homodimer interface

Popis výsledku v původním jazyce

Hydrogen/deuterium (H/D) exchange or chemical cross-linking by soluble carbodiimide (EDC) was employed in combination with high-resolution mass spectrometry (MS) to extend our knowledge about contact surface regions involved in the well-characterized model of interaction between two molecules of human 14-3-3 zeta regulatory protein.The H/D exchange experiment provided low resolution mapping of interaction in the homodimeric 14-3-3 zeta complex. A lower level of deuteration, suggesting structural protection, of two sequential segments has been demonstrated for dimeric 14-3-3 zeta wild type relative to the monomeric mutant 14-3-3 zeta S58D. The N-terminal sequence (the first 27 residues) from one subunit interacts with region alpha C'' and alpha D''-helices (residues 45-98) of the other molecule across the dimer interface. To identify interacting amino acid residues within the studied complex, a chemical cross-linking reaction was carried out to produce the covalent homodimer, which was

Název v anglickém jazyce

The combination of hydrogen/deuterium exchange or chemical cross-linking techniques with mass spectrometry: Mapping of human 14-3-3 zeta homodimer interface

Popis výsledku anglicky

Hydrogen/deuterium (H/D) exchange or chemical cross-linking by soluble carbodiimide (EDC) was employed in combination with high-resolution mass spectrometry (MS) to extend our knowledge about contact surface regions involved in the well-characterized model of interaction between two molecules of human 14-3-3 zeta regulatory protein.The H/D exchange experiment provided low resolution mapping of interaction in the homodimeric 14-3-3 zeta complex. A lower level of deuteration, suggesting structural protection, of two sequential segments has been demonstrated for dimeric 14-3-3 zeta wild type relative to the monomeric mutant 14-3-3 zeta S58D. The N-terminal sequence (the first 27 residues) from one subunit interacts with region alpha C'' and alpha D''-helices (residues 45-98) of the other molecule across the dimer interface. To identify interacting amino acid residues within the studied complex, a chemical cross-linking reaction was carried out to produce the covalent homodimer, which was

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

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)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Journal of Structural Biology

ISSN

1047-8477

e-ISSN

—

Svazek periodika

179

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

10-17

Kód UT WoS článku

000305775400002

EID výsledku v databázi Scopus

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