SrasV1, Main, Exploration, bibRecordById, pubmed:20709084

NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5.

Identifieur interne : 002495 ( Main/Exploration ); précédent : 002494; suivant : 002496

NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5.

Auteurs : Margaret A. Johnson [États-Unis] ; Kristaps Jaudzems ; Kurt Wüthrich

Source :

Journal of molecular biology [ 1089-8638 ] ; 2010.

RBID : pubmed:20709084

Descripteurs français

KwdFr :
- Cinétique, Concentration en ions d'hydrogène, Conformation des protéines, Protéines virales non structurales (), Solutions, Spectroscopie par résonance magnétique (), Structure secondaire des protéines, Virus du SRAS ().
MESH :
- Cinétique, Concentration en ions d'hydrogène, Conformation des protéines, Protéines virales non structurales, Solutions, Spectroscopie par résonance magnétique, Structure secondaire des protéines, Virus du SRAS.

English descriptors

KwdEn :
- Hydrogen-Ion Concentration, Kinetics, Magnetic Resonance Spectroscopy (methods), Protein Conformation, Protein Structure, Secondary, SARS Virus (chemistry), Solutions, Viral Nonstructural Proteins (chemistry).
MESH :
- chemical , chemistry : Viral Nonstructural Proteins.
- chemical : Solutions.
- chemistry : SARS Virus.
- methods : Magnetic Resonance Spectroscopy.
- Hydrogen-Ion Concentration, Kinetics, Protein Conformation, Protein Structure, Secondary.

Abstract

The NMR structure of the severe acute respiratory syndrome coronavirus nonstructural protein (nsp) 7 in aqueous solution at pH 6.5 was determined and compared with the results of previous structure determinations of nsp7 in solution at pH 7.5 and in the crystals of a hexadecameric nsp7/nsp8 complex obtained from a solution at pH 7.5. All three structures contain four helices as the only regular secondary structures, but there are differences in the lengths and sequence locations of the four helices, as well as between the tertiary folds. The present study includes data on conformational equilibria and intramolecular rate processes in nsp7 in solution at pH 6.5, which provide further insights into the polymorphisms implicated by a comparison of the three presently available nsp7 structures.

DOI: 10.1016/j.jmb.2010.07.043
PubMed: 20709084

Affiliations:

Le document en format XML

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<front><div type="abstract" xml:lang="en">The NMR structure of the severe acute respiratory syndrome coronavirus nonstructural protein (nsp) 7 in aqueous solution at pH 6.5 was determined and compared with the results of previous structure determinations of nsp7 in solution at pH 7.5 and in the crystals of a hexadecameric nsp7/nsp8 complex obtained from a solution at pH 7.5. All three structures contain four helices as the only regular secondary structures, but there are differences in the lengths and sequence locations of the four helices, as well as between the tertiary folds. The present study includes data on conformational equilibria and intramolecular rate processes in nsp7 in solution at pH 6.5, which provide further insights into the polymorphisms implicated by a comparison of the three presently available nsp7 structures.</div>
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<country name="États-Unis"><region name="Californie"><name sortKey="Johnson, Margaret A" sort="Johnson, Margaret A" uniqKey="Johnson M" first="Margaret A" last="Johnson">Margaret A. Johnson</name>
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NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5.

NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5.

Source :

Descripteurs français

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

Pour générer des pages wiki

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