SrasV1, Main, Exploration, bibRecord, 002A73

Mesodynamics in the SARS nucleocapsid measured by NMR field cycling.

Identifieur interne : 002A73 ( Main/Exploration ); précédent : 002A72; suivant : 002A74

Mesodynamics in the SARS nucleocapsid measured by NMR field cycling.

Auteurs : Michael W. Clarkson [États-Unis] ; Ming Lei ; Elan Z. Eisenmesser ; Wladimir Labeikovsky ; Alfred Redfield ; Dorothee Kern

Source :

Journal of biomolecular NMR [ 1573-5001 ] ; 2009.

RBID : pubmed:19641854

Descripteurs français

KwdFr :
- Conformation des protéines, Isotopes de l'azote (), Modèles moléculaires, Méthode de Monte-Carlo, Protéines nucléocapside (), Résonance magnétique nucléaire biomoléculaire (), Simulation numérique, Virus du SRAS ().
MESH :
- Conformation des protéines, Isotopes de l'azote, Modèles moléculaires, Méthode de Monte-Carlo, Protéines nucléocapside, Résonance magnétique nucléaire biomoléculaire, Simulation numérique, Virus du SRAS.

English descriptors

KwdEn :
- Computer Simulation, Models, Molecular, Monte Carlo Method, Nitrogen Isotopes (chemistry), Nuclear Magnetic Resonance, Biomolecular (methods), Nucleocapsid Proteins (chemistry), Protein Conformation, SARS Virus (chemistry).
MESH :
- chemical , chemistry : Nitrogen Isotopes, Nucleocapsid Proteins.
- chemistry : SARS Virus.
- methods : Nuclear Magnetic Resonance, Biomolecular.
- Computer Simulation, Models, Molecular, Monte Carlo Method, Protein Conformation.

Abstract

Protein motions on all timescales faster than molecular tumbling are encoded in the spectral density. The dissection of complex protein dynamics is typically performed using relaxation rates determined at high and ultra-high field. Here we expand this range of the spectral density to low fields through field cycling using the nucleocapsid protein of the SARS coronavirus as a model system. The field-cycling approach enables site-specific measurements of R (1) at low fields with the sensitivity and resolution of a high-field magnet. These data, together with high-field relaxation and heteronuclear NOE, provide evidence for correlated rigid-body motions of the entire beta-hairpin, and corresponding motions of adjacent loops with a time constant of 0.8 ns (mesodynamics). MD simulations substantiate these findings and provide direct verification of the time scale and collective nature of these motions.

DOI: 10.1007/s10858-009-9347-6
PubMed: 19641854

Affiliations:

Le document en format XML

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<series><title level="j">Journal of biomolecular NMR</title>
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<term>Nuclear Magnetic Resonance, Biomolecular (methods)</term>
<term>Nucleocapsid Proteins (chemistry)</term>
<term>Protein Conformation</term>
<term>SARS Virus (chemistry)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines</term>
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<term>Protéines nucléocapside ()</term>
<term>Résonance magnétique nucléaire biomoléculaire ()</term>
<term>Simulation numérique</term>
<term>Virus du SRAS ()</term>
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<term>Méthode de Monte-Carlo</term>
<term>Protéines nucléocapside</term>
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<front><div type="abstract" xml:lang="en">Protein motions on all timescales faster than molecular tumbling are encoded in the spectral density. The dissection of complex protein dynamics is typically performed using relaxation rates determined at high and ultra-high field. Here we expand this range of the spectral density to low fields through field cycling using the nucleocapsid protein of the SARS coronavirus as a model system. The field-cycling approach enables site-specific measurements of R (1) at low fields with the sensitivity and resolution of a high-field magnet. These data, together with high-field relaxation and heteronuclear NOE, provide evidence for correlated rigid-body motions of the entire beta-hairpin, and corresponding motions of adjacent loops with a time constant of 0.8 ns (mesodynamics). MD simulations substantiate these findings and provide direct verification of the time scale and collective nature of these motions.</div>
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<country name="États-Unis"><region name="Massachusetts"><name sortKey="Clarkson, Michael W" sort="Clarkson, Michael W" uniqKey="Clarkson M" first="Michael W" last="Clarkson">Michael W. Clarkson</name>
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Mesodynamics in the SARS nucleocapsid measured by NMR field cycling.

Mesodynamics in the SARS nucleocapsid measured by NMR field cycling.

Source :

Descripteurs français

English descriptors

Abstract

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

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