SrasV1, PubMed, Corpus, bibRecord, 001854

Mesodynamics in the SARS nucleocapsid measured by NMR field cycling.

Identifieur interne : 001854 ( PubMed/Corpus ); précédent : 001853; suivant : 001855

Mesodynamics in the SARS nucleocapsid measured by NMR field cycling.

Auteurs : Michael W. Clarkson ; Ming Lei ; Elan Z. Eisenmesser ; Wladimir Labeikovsky ; Alfred Redfield ; Dorothee Kern

Source :

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

RBID : pubmed:19641854

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

Links to Exploration step

pubmed:19641854

Le document en format XML

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<author><name sortKey="Clarkson, Michael W" sort="Clarkson, Michael W" uniqKey="Clarkson M" first="Michael W" last="Clarkson">Michael W. Clarkson</name>
<affiliation><nlm:affiliation>Department of Biochemistry and Howard Hughes Medical Institute, MS009 Brandeis University, Waltham, MA 02452, USA.</nlm:affiliation>
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<author><name sortKey="Lei, Ming" sort="Lei, Ming" uniqKey="Lei M" first="Ming" last="Lei">Ming Lei</name>
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<author><name sortKey="Eisenmesser, Elan Z" sort="Eisenmesser, Elan Z" uniqKey="Eisenmesser E" first="Elan Z" last="Eisenmesser">Elan Z. Eisenmesser</name>
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<author><name sortKey="Labeikovsky, Wladimir" sort="Labeikovsky, Wladimir" uniqKey="Labeikovsky W" first="Wladimir" last="Labeikovsky">Wladimir Labeikovsky</name>
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<author><name sortKey="Redfield, Alfred" sort="Redfield, Alfred" uniqKey="Redfield A" first="Alfred" last="Redfield">Alfred Redfield</name>
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<author><name sortKey="Kern, Dorothee" sort="Kern, Dorothee" uniqKey="Kern D" first="Dorothee" last="Kern">Dorothee Kern</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Mesodynamics in the SARS nucleocapsid measured by NMR field cycling.</title>
<author><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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<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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<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>
</front>
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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 :

English descriptors

Abstract

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki