Accessibility changes within diphtheria toxin T domain when in the functional molten globule state, as determined using hydrogen/deuterium exchange measurements

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F10%3A00340829" target="_blank" >RIV/61388971:_____/10:00340829 - 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

Accessibility changes within diphtheria toxin T domain when in the functional molten globule state, as determined using hydrogen/deuterium exchange measurements

Popis výsledku v původním jazyce

ydrogen/Deuterium exchange coupled to mass spectrometry was used to describe pH driven unfolding of translocation domain from diphtheria toxin. Deuteration kinetics of two states, native-like at pH 7, and molten globule, at pH 4, were followed. In the native like state, helices TH5 and 8 were identified as the core of the protein. Surprisingly, this core is partially preserved even in the molten globule state which is usually characterized by the loss of tertiary structure. In addition, deuteration kinetics at pH 4 discovered surprising behavior of the interconnecting loop TL8-9. This part, which is supposed to be responsible for the insertion of the toxin into the lipid membrane forms oligomerization surface when the membrane is absent. These findingsprovide new insight into self-assembly of bacterial toxins

Název v anglickém jazyce

Accessibility changes within diphtheria toxin T domain when in the functional molten globule state, as determined using hydrogen/deuterium exchange measurements

Popis výsledku anglicky

ydrogen/Deuterium exchange coupled to mass spectrometry was used to describe pH driven unfolding of translocation domain from diphtheria toxin. Deuteration kinetics of two states, native-like at pH 7, and molten globule, at pH 4, were followed. In the native like state, helices TH5 and 8 were identified as the core of the protein. Surprisingly, this core is partially preserved even in the molten globule state which is usually characterized by the loss of tertiary structure. In addition, deuteration kinetics at pH 4 discovered surprising behavior of the interconnecting loop TL8-9. This part, which is supposed to be responsible for the insertion of the toxin into the lipid membrane forms oligomerization surface when the membrane is absent. These findingsprovide new insight into self-assembly of bacterial toxins

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2010

Kód důvěrnosti údajů

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

Název periodika

FEBS Journal

ISSN

1742-464X

e-ISSN

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Svazek periodika

277

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

10

Strana od-do

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Kód UT WoS článku

000273723200013

EID výsledku v databázi Scopus

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