Protein Surface and Core Dynamics Show Concerted Hydration‐Dependent Activation
Identifieur interne : 004984 ( Main/Exploration ); précédent : 004983; suivant : 004985Protein 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 International Edition [ 1433-7851 ] ; 2013-01-07.
English descriptors
- KwdEn :
- Angewandte communications, Atomic groups, Biophys, Calbindin, Chem, Dynamical transition, Dynamics, Hydrated, Hydrated samples, Hydration, Hydrogen atoms, Hydrophobic core, Leucine residues, Localized diffusion, Lysine, Lysine residues, Methyl, Methyl groups, Neutron, Phys, Protein dynamics, Protein energy landscape, Protonated, Protonated lysine residues, Protonated methyl groups, Sample preparation, Side chains, Square displacements, Temperature range, Transition temperature, Verlag gmbh, Water molecules, Weinheim angew, Wide temperature range, Zaccai.
- Teeft :
- Angewandte communications, Atomic groups, Biophys, Calbindin, Chem, Dynamical transition, Dynamics, Hydrated, Hydrated samples, Hydration, Hydrogen atoms, Hydrophobic core, Leucine residues, Localized diffusion, Lysine, Lysine residues, Methyl, Methyl groups, Neutron, Phys, Protein dynamics, Protein energy landscape, Protonated, Protonated lysine residues, Protonated methyl groups, Sample preparation, Side chains, Square displacements, Temperature range, Transition temperature, Verlag gmbh, Water molecules, Weinheim angew, Wide temperature range, Zaccai.
Abstract
By specifically labeling leucine/valine methyl groups and lysine side chains “inside” and “outside” dynamics of proteins on the nanosecond timescale are compared using neutron scattering (see picture). Surprisingly, both groups display similar dynamics as a function of temperature, and the buried hydrophobic core is sensitive to hydration and undergoes a dynamical transition.
Url:
DOI: 10.1002/anie.201205898
Affiliations:
- Australie, Danemark, France, Pays-Bas
- Auvergne-Rhône-Alpes, Groningue (province), Rhône-Alpes
- Grenoble, Groningue (ville)
- Université Joseph Fourier, Université de Grenoble, Université de Groningue
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Le document en format XML
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<front><div type="abstract">By specifically labeling leucine/valine methyl groups and lysine side chains “inside” and “outside” dynamics of proteins on the nanosecond timescale are compared using neutron scattering (see picture). Surprisingly, both groups display similar dynamics as a function of temperature, and the buried hydrophobic core is sensitive to hydration and undergoes a dynamical transition.</div>
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