About: Accessibility Changes within Diphtheria Toxin T Domain upon Membrane Penetration Probed by Hydrogen Exchange and Mass Spectrometry

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About: Accessibility Changes within Diphtheria Toxin T Domain upon Membrane Penetration Probed by Hydrogen Exchange and Mass Spectrometry Goto Sponge NotDistinct Permalink

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	The translocation domain of diphtheria toxin inserts in membrane and becomes functional when the pH inside endosomes is acid. At that stage, the domain is in a partially folded state; this prevents the use of high-resolution methods for the characterization of its functional structure. On that purpose, we report here the use of hydrogen/deuterium exchange experiments coupled to mass spectrometry. The conformation changes during the different steps of insertion into lipid bilayer are monitored with a resolution of few residues. Three parts of the translocation domain can be distinguished. With a high protection against exchange, the C-terminal hydrophobic helical hairpin is embedded in the membrane. Despite a lower protection, a significant effect in the presence of lipid vesicles shows that the N-terminal part is in interaction with the membrane interface The translocation domain of diphtheria toxin inserts in membrane and becomes functional when the pH inside endosomes is acid. At that stage, the domain is in a partially folded state; this prevents the use of high-resolution methods for the characterization of its functional structure. On that purpose, we report here the use of hydrogen/deuterium exchange experiments coupled to mass spectrometry. The conformation changes during the different steps of insertion into lipid bilayer are monitored with a resolution of few residues. Three parts of the translocation domain can be distinguished. With a high protection against exchange, the C-terminal hydrophobic helical hairpin is embedded in the membrane. Despite a lower protection, a significant effect in the presence of lipid vesicles shows that the N-terminal part is in interaction with the membrane interface (en)
Title	Accessibility Changes within Diphtheria Toxin T Domain upon Membrane Penetration Probed by Hydrogen Exchange and Mass Spectrometry Accessibility Changes within Diphtheria Toxin T Domain upon Membrane Penetration Probed by Hydrogen Exchange and Mass Spectrometry (en)
skos:prefLabel	Accessibility Changes within Diphtheria Toxin T Domain upon Membrane Penetration Probed by Hydrogen Exchange and Mass Spectrometry Accessibility Changes within Diphtheria Toxin T Domain upon Membrane Penetration Probed by Hydrogen Exchange and Mass Spectrometry (en)
skos:notation	RIV/61388971:_____/11:00372742!RIV12-AV0-61388971
http://linked.open...avai/predkladatel	Mikrobiologický ústav AV ČR, v.v.i.
http://linked.open...avai/riv/aktivita	Z
http://linked.open...avai/riv/aktivity	Z(AV0Z50200510)
http://linked.open...iv/cisloPeriodika	1
http://linked.open...vai/riv/dodaniDat	2012
http://linked.open...aciTvurceVysledku	Kavan, Daniel Man, Petr
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Mikrobiologický ústav AV ČR, v. v. i.
http://linked.open...dnocenehoVysledku	184387
http://linked.open...ai/riv/idVysledku	RIV/61388971:_____/11:00372742
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	diphtheria toxin; translocation domain; protein/membrane interactions (en)
http://linked.open.../riv/klicoveSlovo	diphtheria toxin protein/membrane interactions translocation domain
http://linked.open...odStatuVydavatele	GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV	[CB436C43C874]
http://linked.open...i/riv/nazevZdroje	Journal of Molecular Biology
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	2 (xsd:int)
http://linked.open...cetTvurcuVysledku	8 (xsd:int)
http://linked.open...UplatneniVysledku	2011
http://linked.open...v/svazekPeriodika	414
http://linked.open...iv/tvurceVysledku	Forest, E. Forge, V. Gillet, D. Kavan, Daniel Man, Petr Montagner, C. Pichard, S. Vitrac, H.
http://linked.open...ain/vavai/riv/wos	000297778800010
http://linked.open...n/vavai/riv/zamer	Microorganisms in Research and Biotechnology
issn	0022-2836
number of pages	12 (xsd:int)
http://bibframe.org/vocab/doi	10.1016/j.jmb.2011.09.042
is http://linked.open...avai/riv/vysledek of	Accessibility Changes within Diphtheria Toxin T Domain upon Membrane Penetration Probed by Hydrogen Exchange and Mass Spectrometry Accessibility Changes within Diphtheria Toxin T Domain upon Membrane Penetration Probed by Hydrogen Exchange and Mass Spectrometry

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