Počet záznamů: 1
Accessibility changes within diphtheria toxin T domain when in the functional molten globule state, as determined using hydrogen/deuterium exchange measurements
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SYSNO ASEP 0340829 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Accessibility changes within diphtheria toxin T domain when in the functional molten globule state, as determined using hydrogen/deuterium exchange measurements Tvůrce(i) Man, Petr (MBU-M) RID, ORCID
Montagner, C. (FR)
Vitrac, H. (FR)
Kavan, Daniel (MBU-M) RID, ORCID
Pichard, S. (FR)
Gillet, D. (FR)
Forest, E. (FR)
Forge, V. (FR)Zdroj.dok. FEBS Journal - ISSN 1742-464X
Roč. 277, č. 3 (2010), s. 653-662Poč.str. 10 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova diphtheria toxin ; hydrogen/deuterium exchanges ; mass spectrometry Vědní obor RIV CE - Biochemie CEZ AV0Z50200510 - MBU-M (2005-2011) UT WOS 000273723200013 DOI 10.1111/j.1742-4658.2009.07511.x Anotace 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 findings provide new insight into self-assembly of bacterial toxins Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2010
Počet záznamů: 1