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

Result code in 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>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

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

Original language description

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

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

CE - Biochemistry

OECD FORD branch

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Project

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Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2010

Confidentiality

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

Name of the periodical

FEBS Journal

ISSN

1742-464X

e-ISSN

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Volume of the periodical

277

Issue of the periodical within the volume

3

Country of publishing house

GB - UNITED KINGDOM

Number of pages

10

Pages from-to

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UT code for WoS article

000273723200013

EID of the result in the Scopus database

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