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About:
In vitro biochemical and thermodynamic characterization of nucleocapsid protein of SARS
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schema:ScholarlyArticle
, within Data Space :
covidontheweb.inria.fr
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Type:
Academic Article
research paper
schema:ScholarlyArticle
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type
Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
has title
In vitro biochemical and thermodynamic characterization of nucleocapsid protein of SARS
Creator
Jiang, Hualiang
Chen, Jing
Luo, Haibin
Peng, Shuying
Shen, Jianhua
Shen, Xu
Sun, Tao
Wang, Yuan
Xie, Youhua
Yang, Yiming
Ye, Fei
Li, Guowei
Du, Yi
Yue, Liduo
Source
Elsevier; Medline; PMC
abstract
Abstract The major biochemical and thermodynamic features of nucelocapsid protein of SARS coronavirus (SARS_NP) were characterized by use of non-denatured gel electrophoresis, size-exclusion chromatographic and surface plasmon resonance (SPR) techniques. The results showed that SARS_NP existed in vitro as oligomer, more probably dimer, as the basic functional unit. This protein shows its maximum conformational stability near pH 9.0, and it seems that its oligomer dissociation and protein unfolding occur simultaneously. Thermal-induced unfolding for SARS_NP was totally irreversible. Both the thermal and chemical denaturant-induced denaturation analyses showed that oligomeric SARS_NP unfolds and refolds through a two-state model, and the electrostatic interactions among the charge groups of SARS_NP made a significant contribution to its conformational stability.
has issue date
2004-12-01
(
xsd:dateTime
)
bibo:doi
10.1016/j.bpc.2004.06.008
bibo:pmid
15501572
has license
els-covid
sha1sum (hex)
3a5991c5ef4b6910b4220151a8978b01291afe84
schema:url
https://doi.org/10.1016/j.bpc.2004.06.008
resource representing a document's title
In vitro biochemical and thermodynamic characterization of nucleocapsid protein of SARS
has PubMed Central identifier
PMC7116930
has PubMed identifier
15501572
schema:publication
Biophysical Chemistry
resource representing a document's body
covid:3a5991c5ef4b6910b4220151a8978b01291afe84#body_text
is
schema:about
of
named entity 'surface plasmon'
named entity 'functional unit'
named entity 'conformational'
named entity 'resonance'
covid:arg/3a5991c5ef4b6910b4220151a8978b01291afe84
named entity 'thermodynamic'
named entity 'SARS coronavirus'
named entity 'SPR'
named entity 'chromatographic'
named entity 'thermal'
named entity 'protein'
named entity 'unfolded'
named entity 'resonance'
named entity 'chemical'
named entity 'unfolding'
named entity 'protein'
named entity 'IPTG'
named entity 'denaturation'
named entity 'denatured'
named entity 'nucleocapsid protein'
named entity 'dimer'
named entity 'SARS'
named entity 'SARS'
named entity 'unfolded states'
named entity 'nucleocapsid protein'
named entity 'denatured protein'
named entity '0.45'
named entity 'urea'
named entity 'SARS'
named entity 'ampicillin'
named entity 'SARS'
named entity 'reverse transcription'
named entity 'molecular weight'
named entity 'pH 8'
named entity 'SARS'
named entity 'NaCl'
named entity 'SPR'
named entity 'kcal'
named entity 'hepatitis B virus'
named entity 'protein'
named entity 'ionic character'
named entity 'guanidine hydrochloride'
named entity 'pH 11'
named entity '11.0'
named entity 'genome sequencing'
named entity 'chromatographic'
named entity 'fluorescent'
named entity 'alkaline'
named entity 'SARS'
named entity 'virus particle'
named entity 'native gel'
named entity 'tryptophan fluorescence'
named entity '10.0'
named entity 'nucleocapsid protein'
named entity 'self-assemble'
named entity 'SARS'
named entity 'polymer'
named entity 'protein refolding'
named entity 'affinity column'
named entity 'SPR'
named entity 'self-assembly'
named entity 'far-UV'
named entity 'gel electrophoresis'
named entity 'envelope proteins'
named entity 'SARS'
named entity 'oligomer'
named entity 'lysozyme'
named entity 'denaturation'
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