AustralieFrV1, Main, Exploration, bibRecord, 004983

Protein Surface and Core Dynamics Show Concerted Hydration‐Dependent Activation

Identifieur interne : 004983 ( Main/Exploration ); précédent : 004982; suivant : 004984

Protein Surface and Core Dynamics Show Concerted Hydration‐Dependent Activation

Auteurs : Kathleen Wood [Australie, Pays-Bas] ; François-Xavier Gallat [France] ; Renee Otten [Pays-Bas] ; Auke J. Van Eel [Pays-Bas] ; Mathilde Lethier [France] ; Lambert Van Ijck [France] ; Martine Moulin [France] ; Michael Haertlein [France] ; Martin Weik [France] ; Frans A. A. Mulder [Danemark, Pays-Bas]

Source :

Angewandte Chemie [ 0044-8249 ] ; 2013-01-07.

RBID : ISTEX:AFC66ECEDCC7B3B1B12DED41A3D30BBA4E01AB5E

English descriptors

Abstract

Durch spezifische Markierung der Leucin/Valin‐Methylgruppen und Lysin‐Seitenketten kann die innere und die äußere Dynamik von Proteinen (siehe Bild) mittels Neutronenstreuung auf der Nanosekunden‐Zeitskala verglichen werden. Überraschenderweise zeigen beide Gruppen eine ähnliche temperaturabhängige Dynamik, und der verborgene hydrophobe Kern reagiert empfindlich auf Hydratisierung und weist einen dynamischen Übergang auf.

Url:

https://api.istex.fr/document/AFC66ECEDCC7B3B1B12DED41A3D30BBA4E01AB5E/fulltext/pdf

DOI: 10.1002/ange.201205898

Affiliations:

Links toward previous steps (curation, corpus...)

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to stream Istex, to step Curation: 002154
to stream Istex, to step Checkpoint: 000293
to stream Main, to step Merge: 004B07
to stream Main, to step Curation: 004983

Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Angewandte zuschriften</term>
<term>Atomic groups</term>
<term>Biophys</term>
<term>Calbindin</term>
<term>Chem</term>
<term>Dynamical transition</term>
<term>Dynamics</term>
<term>Hydrated</term>
<term>Hydrated samples</term>
<term>Hydration</term>
<term>Hydrogen atoms</term>
<term>Hydrophobic core</term>
<term>Leucine residues</term>
<term>Localized diffusion</term>
<term>Lysine</term>
<term>Lysine residues</term>
<term>Methyl</term>
<term>Methyl groups</term>
<term>Neutron</term>
<term>Phys</term>
<term>Protein dynamics</term>
<term>Protein energy landscape</term>
<term>Protonated</term>
<term>Protonated lysine residues</term>
<term>Protonated methyl groups</term>
<term>Sample preparation</term>
<term>Side chains</term>
<term>Square displacements</term>
<term>Temperature range</term>
<term>Transition temperature</term>
<term>Verlag gmbh</term>
<term>Water molecules</term>
<term>Weinheim angew</term>
<term>Wide temperature range</term>
<term>Zaccai</term>
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<term>Atomic groups</term>
<term>Biophys</term>
<term>Calbindin</term>
<term>Chem</term>
<term>Dynamical transition</term>
<term>Dynamics</term>
<term>Hydrated</term>
<term>Hydrated samples</term>
<term>Hydration</term>
<term>Hydrogen atoms</term>
<term>Hydrophobic core</term>
<term>Leucine residues</term>
<term>Localized diffusion</term>
<term>Lysine</term>
<term>Lysine residues</term>
<term>Methyl</term>
<term>Methyl groups</term>
<term>Neutron</term>
<term>Phys</term>
<term>Protein dynamics</term>
<term>Protein energy landscape</term>
<term>Protonated</term>
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<term>Protonated methyl groups</term>
<term>Sample preparation</term>
<term>Side chains</term>
<term>Square displacements</term>
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<term>Transition temperature</term>
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<front><div type="abstract">Durch spezifische Markierung der Leucin/Valin‐Methylgruppen und Lysin‐Seitenketten kann die innere und die äußere Dynamik von Proteinen (siehe Bild) mittels Neutronenstreuung auf der Nanosekunden‐Zeitskala verglichen werden. Überraschenderweise zeigen beide Gruppen eine ähnliche temperaturabhängige Dynamik, und der verborgene hydrophobe Kern reagiert empfindlich auf Hydratisierung und weist einen dynamischen Übergang auf.</div>
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<li>Groningue (province)</li>
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<settlement><li>Grenoble</li>
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<name sortKey="Gallat, Francois Avier" sort="Gallat, Francois Avier" uniqKey="Gallat F" first="François-Xavier" last="Gallat">François-Xavier Gallat</name>
<name sortKey="Haertlein, Michael" sort="Haertlein, Michael" uniqKey="Haertlein M" first="Michael" last="Haertlein">Michael Haertlein</name>
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<name sortKey="Weik, Martin" sort="Weik, Martin" uniqKey="Weik M" first="Martin" last="Weik">Martin Weik</name>
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<country name="Danemark"><noRegion><name sortKey="Mulder, Frans A A" sort="Mulder, Frans A A" uniqKey="Mulder F" first="Frans A. A." last="Mulder">Frans A. A. Mulder</name>
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<name sortKey="Mulder, Frans A A" sort="Mulder, Frans A A" uniqKey="Mulder F" first="Frans A. A." last="Mulder">Frans A. A. Mulder</name>
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	Serveur d'exploration sur les relations entre la France et l'Australie
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Serveur d'exploration sur les relations entre la France et l'Australie

Protein Surface and Core Dynamics Show Concerted Hydration‐Dependent Activation

Protein Surface and Core Dynamics Show Concerted Hydration‐Dependent Activation

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri