SrasV1, PubMed, Checkpoint, bibRecord, 001754

Thermostability of the N-terminal RNA-binding domain of the SARS-CoV nucleocapsid protein: experiments and numerical simulations.

Identifieur interne : 001754 ( PubMed/Checkpoint ); précédent : 001753; suivant : 001755

Thermostability of the N-terminal RNA-binding domain of the SARS-CoV nucleocapsid protein: experiments and numerical simulations.

Auteurs : Huey-Jen Fang [Taïwan] ; Yong-Zhong Chen ; Mai Suan Li ; Ming-Chya Wu ; Chun-Ling Chang ; Chung-Ke Chang ; Yen-Lan Hsu ; Tai-Huang Huang ; Hueih-Min Chen ; Tian-Yow Tsong ; Chin-Kun Hu

Source :

Biophysical journal [ 1542-0086 ] ; 2009.

RBID : pubmed:19254548

Descripteurs français

English descriptors

KwdEn :
- Algorithms, Calorimetry, Differential Scanning, Circular Dichroism, Computer Simulation, Models, Chemical, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (metabolism), Protein Folding, Protein Stability, Protein Structure, Tertiary, RNA (metabolism), SARS Virus (chemistry), Temperature, Thermodynamics, Transition Temperature.
MESH :
- chemical , chemistry : Nucleocapsid Proteins.
- chemical , metabolism : Nucleocapsid Proteins, RNA.
- chemistry : SARS Virus.
- Algorithms, Calorimetry, Differential Scanning, Circular Dichroism, Computer Simulation, Models, Chemical, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Folding, Protein Stability, Protein Structure, Tertiary, Temperature, Thermodynamics, Transition Temperature.

Abstract

Differential scanning calorimetry, circular dichroism spectroscopy, nuclear magnetic resonance spectroscopy, and numerical simulations were used to study the thermostability of the N-terminal RNA-binding domain (RBD) of the SARS-CoV nucleocapsid protein. The transition temperature of the RBD in a mixing buffer, composed of glycine, sodium acetate, and sodium phosphate with 100 mM sodium chloride, at pH 6.8, determined by differential scanning calorimetry and circular dichroism, is 48.74 degrees C. Experimental results showed that the thermal-induced unfolding-folding transition of the RBD follows a two-state model with a reversibility >90%. Using a simple Gō-like model and Langevin dynamics we have shown that, in agreement with our experiments, the folding of the RBD is two-state. Theoretical estimates of thermodynamic quantities are in reasonable agreement with the experiments. Folding and thermal unfolding pathways of the RBD also were experimentally and numerically studied in detail. It was shown that the strand beta(1) from the N-terminal folds last and unfolds first, while the remaining beta-strands fold/unfold cooperatively.

DOI: 10.1016/j.bpj.2008.10.045
PubMed: 19254548

Affiliations:

Taïwan

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pubmed:19254548

Le document en format XML

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<front><div type="abstract" xml:lang="en">Differential scanning calorimetry, circular dichroism spectroscopy, nuclear magnetic resonance spectroscopy, and numerical simulations were used to study the thermostability of the N-terminal RNA-binding domain (RBD) of the SARS-CoV nucleocapsid protein. The transition temperature of the RBD in a mixing buffer, composed of glycine, sodium acetate, and sodium phosphate with 100 mM sodium chloride, at pH 6.8, determined by differential scanning calorimetry and circular dichroism, is 48.74 degrees C. Experimental results showed that the thermal-induced unfolding-folding transition of the RBD follows a two-state model with a reversibility >90%. Using a simple Gō-like model and Langevin dynamics we have shown that, in agreement with our experiments, the folding of the RBD is two-state. Theoretical estimates of thermodynamic quantities are in reasonable agreement with the experiments. Folding and thermal unfolding pathways of the RBD also were experimentally and numerically studied in detail. It was shown that the strand beta(1) from the N-terminal folds last and unfolds first, while the remaining beta-strands fold/unfold cooperatively.</div>
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<Abstract><AbstractText>Differential scanning calorimetry, circular dichroism spectroscopy, nuclear magnetic resonance spectroscopy, and numerical simulations were used to study the thermostability of the N-terminal RNA-binding domain (RBD) of the SARS-CoV nucleocapsid protein. The transition temperature of the RBD in a mixing buffer, composed of glycine, sodium acetate, and sodium phosphate with 100 mM sodium chloride, at pH 6.8, determined by differential scanning calorimetry and circular dichroism, is 48.74 degrees C. Experimental results showed that the thermal-induced unfolding-folding transition of the RBD follows a two-state model with a reversibility >90%. Using a simple Gō-like model and Langevin dynamics we have shown that, in agreement with our experiments, the folding of the RBD is two-state. Theoretical estimates of thermodynamic quantities are in reasonable agreement with the experiments. Folding and thermal unfolding pathways of the RBD also were experimentally and numerically studied in detail. It was shown that the strand beta(1) from the N-terminal folds last and unfolds first, while the remaining beta-strands fold/unfold cooperatively.</AbstractText>
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<name sortKey="Chang, Chung Ke" sort="Chang, Chung Ke" uniqKey="Chang C" first="Chung-Ke" last="Chang">Chung-Ke Chang</name>
<name sortKey="Chen, Hueih Min" sort="Chen, Hueih Min" uniqKey="Chen H" first="Hueih-Min" last="Chen">Hueih-Min Chen</name>
<name sortKey="Chen, Yong Zhong" sort="Chen, Yong Zhong" uniqKey="Chen Y" first="Yong-Zhong" last="Chen">Yong-Zhong Chen</name>
<name sortKey="Hsu, Yen Lan" sort="Hsu, Yen Lan" uniqKey="Hsu Y" first="Yen-Lan" last="Hsu">Yen-Lan Hsu</name>
<name sortKey="Hu, Chin Kun" sort="Hu, Chin Kun" uniqKey="Hu C" first="Chin-Kun" last="Hu">Chin-Kun Hu</name>
<name sortKey="Huang, Tai Huang" sort="Huang, Tai Huang" uniqKey="Huang T" first="Tai-Huang" last="Huang">Tai-Huang Huang</name>
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Thermostability of the N-terminal RNA-binding domain of the SARS-CoV nucleocapsid protein: experiments and numerical simulations.

Thermostability of the N-terminal RNA-binding domain of the SARS-CoV nucleocapsid protein: experiments and numerical simulations.

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