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In vitro biochemical and thermodynamic characterization of nucleocapsid protein of SARS

Identifieur interne : 005295 ( Main/Exploration ); précédent : 005294; suivant : 005296

In vitro biochemical and thermodynamic characterization of nucleocapsid protein of SARS

Auteurs : Haibin Luo [République populaire de Chine] ; Fei Ye [République populaire de Chine] ; Tao Sun [République populaire de Chine] ; Liduo Yue [République populaire de Chine] ; Shuying Peng [République populaire de Chine] ; Jing Chen [République populaire de Chine] ; Guowei Li [République populaire de Chine] ; Yi Du [République populaire de Chine] ; Youhua Xie [République populaire de Chine] ; Yiming Yang [République populaire de Chine] ; Jianhua Shen [République populaire de Chine] ; Yuan Wang [République populaire de Chine] ; Xu Shen [République populaire de Chine] ; Hualiang Jiang [République populaire de Chine]

Source :

RBID : PMC:7116930

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.


Url:
DOI: 10.1016/j.bpc.2004.06.008
PubMed: 15501572
PubMed Central: 7116930


Affiliations:


Links toward previous steps (curation, corpus...)


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<author>
<name sortKey="Wang, Yuan" sort="Wang, Yuan" uniqKey="Wang Y" first="Yuan" last="Wang">Yuan Wang</name>
<affiliation wicri:level="1">
<nlm:aff id="aff3">Shanghai Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>Shanghai Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031</wicri:regionArea>
<wicri:noRegion>Shanghai 200031</wicri:noRegion>
</affiliation>
</author>
<author>
<name sortKey="Shen, Xu" sort="Shen, Xu" uniqKey="Shen X" first="Xu" last="Shen">Xu Shen</name>
<affiliation wicri:level="1">
<nlm:aff id="aff1">Drug Discovery and Design Center, State Key Lab of Drug Research, Shanghai Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 201203, China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>Drug Discovery and Design Center, State Key Lab of Drug Research, Shanghai Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 201203</wicri:regionArea>
<wicri:noRegion>Shanghai 201203</wicri:noRegion>
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</author>
<author>
<name sortKey="Jiang, Hualiang" sort="Jiang, Hualiang" uniqKey="Jiang H" first="Hualiang" last="Jiang">Hualiang Jiang</name>
<affiliation wicri:level="1">
<nlm:aff id="aff1">Drug Discovery and Design Center, State Key Lab of Drug Research, Shanghai Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 201203, China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>Drug Discovery and Design Center, State Key Lab of Drug Research, Shanghai Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 201203</wicri:regionArea>
<wicri:noRegion>Shanghai 201203</wicri:noRegion>
</affiliation>
</author>
</analytic>
<series>
<title level="j">Biophysical Chemistry</title>
<idno type="ISSN">0301-4622</idno>
<idno type="eISSN">1873-4200</idno>
<imprint>
<date when="2004">2004</date>
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</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc>
<textClass></textClass>
</profileDesc>
</teiHeader>
<front>
<div type="abstract" xml:lang="en">
<p>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.</p>
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<affiliations>
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</tree>
</affiliations>
</record>

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