About: Thermostability of the N-Terminal RNA-Binding Domain of the SARS-CoV Nucleocapsid Protein: Experiments and Numerical Simulations

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About: Thermostability of the N-Terminal RNA-Binding Domain of the SARS-CoV Nucleocapsid Protein: Experiments and Numerical Simulations Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Thermostability of the N-Terminal RNA-Binding Domain of the SARS-CoV Nucleocapsid Protein: Experiments and Numerical Simulations
Creator	Hsu, Yen-Lan Chang, Chung-Ke Huang, Tai-Huang Hu, Chin-Kun Wu, Ming-Chya Chang, Chun-Ling Chen, Hueih-Min Chen, Yong-Zhong Fang, Huey-Jen Li, Mai Tsong, Tian-Yow
Source	Elsevier; Medline; PMC
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°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 β(1) from the N-terminal folds last and unfolds first, while the remaining β-strands fold/unfold cooperatively.
has issue date	2009-03-01(xsd:dateTime)
bibo:doi	10.1016/j.bpj.2008.10.045
bibo:pmid	19254548
has license	hybrid-oa
sha1sum (hex)	a51943a6b6527dd8f62bc27c061a6371fd045dce
schema:url	https://doi.org/10.1016/j.bpj.2008.10.045
resource representing a document's title	Thermostability of the N-Terminal RNA-Binding Domain of the SARS-CoV Nucleocapsid Protein: Experiments and Numerical Simulations
has PubMed Central identifier	PMC2717332
has PubMed identifier	19254548
schema:publication	Biophysical Journal
resource representing a document's body	covid:a51943a6b6527dd8f62bc27c061a6371fd045dce#body_text
is schema:about of	named entity 'BINDING' named entity 'N-TERMINAL ' named entity 'SARS-COV' named entity 'STATE' named entity 'TRANSITION TEMPERATURE' named entity 'GLYCINE' named entity 'USING' named entity 'CIRCULAR DICHROISM' named entity 'USED' named entity 'STUDY' named entity 'PATHWAYS' named entity 'AGREEMENT' named entity 'THE STRAND' named entity 'DETERMINED BY' named entity 'SARS-COV' named entity 'DYNAMICS' named entity 'MIXING' named entity 'RNA' named entity 'REVERSIBILITY' named entity 'EXPERIMENTS' named entity 'NUCLEOCAPSID PROTEIN' named entity 'DOMAIN' named entity 'FOLDING' named entity 'INDUCED' named entity 'BINDING' named entity 'HAVE' named entity 'OUR' named entity 'NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY' named entity 'SODIUM ACETATE' named entity 'SODIUM PHOSPHATE' named entity 'THERMAL' named entity 'COMPOSED OF' named entity 'THEORETICAL' named entity 'FOLDS' named entity 'CIRCULAR DICHROISM SPECTROSCOPY' named entity 'THERMOSTABILITY' named entity 'TRANSITION' named entity '100' named entity 'QUANTITIES' named entity 'UNFOLDING' named entity 'BUFFER' named entity 'NUCLEOCAPSID PROTEIN' named entity 'DOMAIN' named entity 'THERMODYNAMIC' named entity 'N-TERMINAL ' named entity 'RNA' named entity 'SIMPLE' named entity 'ESTIMATES' named entity 'RBD' named entity 'EXPERIMENTAL RESULTS' named entity 'FOLD' named entity 'LIKE' named entity 'NUMERICAL SIMULATIONS' named entity 'REMAINING' named entity 'MODEL' named entity 'FOLLOWS' named entity 'DIFFERENTIAL SCANNING CALORIMETRY' named entity 'SODIUM CHLORIDE' named entity 'NUMERICAL SIMULATIONS' named entity 'THERMOSTABILITY' named entity 'EXPERIMENTS' named entity 'transition temperature' named entity 'thermodynamic' named entity 'circular dichroism' named entity 'N-terminal' named entity 'circular dichroism spectroscopy' named entity 'RBD' named entity 'RBD' named entity 'sodium phosphate' named entity 'glycine' named entity 'numerical simulations'

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