Self-Assembling Process of Cylindrical Virus Coat Proteins as Observed by Synchrotron Small-Angle X-Ray Scattering
Identifieur interne : 000873 ( Istex/Corpus ); précédent : 000872; suivant : 000874Self-Assembling Process of Cylindrical Virus Coat Proteins as Observed by Synchrotron Small-Angle X-Ray Scattering
Auteurs : Yoh Sano ; Hideo Inoue ; Kanji Kajiwara ; Hiroshi Urakawa ; Yuzuru HiragiSource :
- The Journal of Biochemistry [ 0021-924X ] ; 1994.
Abstract
The self-assembly process of cucumber green mottle mosaic virus (CGMMV) protein and tobacco mosaic virus (TMV) protein was examined by the thermodynamic analysis of small-angle X-ray scattering (SAXS) data. Each polymerization step of the coat proteins was assumed to be specified by a single equilibrium constant, and the equilibrium constant was evaluated by fitting the size and shape of the constituents observed by SAXS to those calculated from an assumed polymerization scheme. The logarithmic plots of the equilibrium constant against the inverse of temperature were fitted with a straight line at each buffer concentration and the thermodynamic quantities were evaluated from its intercept (yielding entropy) and slope (yielding enthalpy). The enthalpy and entropy values of TMV protein were found to be independent of buffer concentration, whereas those of CGMMV protein depended strongly on buffer concentration. In the limit, as ionic strength tends to infinity, both the enthalpy and entropy values of CGMMV protein approach those of TMV protein. The higher negative surface charge of CGMMV protein is considered to be responsible for the formation of stable single-layered disks, and for the slow polymerization process even at higher temperature and higher buffer concentrations.
Url:
DOI: 10.1093/oxfordjournals.jbchem.a124457
Links to Exploration step
ISTEX:C5675519F6EAC4B43F8C17D3EB36E96F48E7525ELe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Self-Assembling Process of Cylindrical Virus Coat Proteins as Observed by Synchrotron Small-Angle X-Ray Scattering</title><author><name sortKey="Sano, Yoh" sort="Sano, Yoh" uniqKey="Sano Y" first="Yoh" last="Sano">Yoh Sano</name><affiliation><mods:affiliation>National Food Research Institute Tsukuba, Ibaraki 305</mods:affiliation></affiliation></author><author><name sortKey="Inoue, Hideo" sort="Inoue, Hideo" uniqKey="Inoue H" first="Hideo" last="Inoue">Hideo Inoue</name><affiliation><mods:affiliation>Shimadzu Corporation Nakagyo-ku, Kyoto 604</mods:affiliation></affiliation></author><author><name sortKey="Kajiwara, Kanji" sort="Kajiwara, Kanji" uniqKey="Kajiwara K" first="Kanji" last="Kajiwara">Kanji Kajiwara</name><affiliation><mods:affiliation>Faculty of Engineering and Design, Kyoto Institute of Technology Sakyo-ku, Kyoto 606</mods:affiliation></affiliation></author><author><name sortKey="Urakawa, Hiroshi" sort="Urakawa, Hiroshi" uniqKey="Urakawa H" first="Hiroshi" last="Urakawa">Hiroshi Urakawa</name><affiliation><mods:affiliation>Faculty of Engineering and Design, Kyoto Institute of Technology Sakyo-ku, Kyoto 606</mods:affiliation></affiliation></author><author><name sortKey="Hiragi, Yuzuru" sort="Hiragi, Yuzuru" uniqKey="Hiragi Y" first="Yuzuru" last="Hiragi">Yuzuru Hiragi</name><affiliation><mods:affiliation>Institute for Chemical Research, Kyoto University Uji, Kyoto 611</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:C5675519F6EAC4B43F8C17D3EB36E96F48E7525E</idno><date when="1994" year="1994">1994</date><idno type="doi">10.1093/oxfordjournals.jbchem.a124457</idno><idno type="url">https://api.istex.fr/ark:/67375/HXZ-2J964QTQ-V/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000873</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000873</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main">Self-Assembling Process of Cylindrical Virus Coat Proteins as Observed by Synchrotron Small-Angle X-Ray Scattering<ref type="fn" target="#fn1"><hi rend="superscript">1</hi></ref></title><author><name sortKey="Sano, Yoh" sort="Sano, Yoh" uniqKey="Sano Y" first="Yoh" last="Sano">Yoh Sano</name><affiliation><mods:affiliation>National Food Research Institute Tsukuba, Ibaraki 305</mods:affiliation></affiliation></author><author><name sortKey="Inoue, Hideo" sort="Inoue, Hideo" uniqKey="Inoue H" first="Hideo" last="Inoue">Hideo Inoue</name><affiliation><mods:affiliation>Shimadzu Corporation Nakagyo-ku, Kyoto 604</mods:affiliation></affiliation></author><author><name sortKey="Kajiwara, Kanji" sort="Kajiwara, Kanji" uniqKey="Kajiwara K" first="Kanji" last="Kajiwara">Kanji Kajiwara</name><affiliation><mods:affiliation>Faculty of Engineering and Design, Kyoto Institute of Technology Sakyo-ku, Kyoto 606</mods:affiliation></affiliation></author><author><name sortKey="Urakawa, Hiroshi" sort="Urakawa, Hiroshi" uniqKey="Urakawa H" first="Hiroshi" last="Urakawa">Hiroshi Urakawa</name><affiliation><mods:affiliation>Faculty of Engineering and Design, Kyoto Institute of Technology Sakyo-ku, Kyoto 606</mods:affiliation></affiliation></author><author><name sortKey="Hiragi, Yuzuru" sort="Hiragi, Yuzuru" uniqKey="Hiragi Y" first="Yuzuru" last="Hiragi">Yuzuru Hiragi</name><affiliation><mods:affiliation>Institute for Chemical Research, Kyoto University Uji, Kyoto 611</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">The Journal of Biochemistry</title><idno type="eISSN">-</idno><idno type="ISSN">0021-924X</idno><imprint><publisher>Oxford University Press</publisher><date type="published">1994</date><biblScope unit="vol">115</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="1058">1058</biblScope><biblScope unit="page" to="1063">1063</biblScope></imprint><idno type="ISSN">0021-924X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0021-924X</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">The self-assembly process of cucumber green mottle mosaic virus (CGMMV) protein and tobacco mosaic virus (TMV) protein was examined by the thermodynamic analysis of small-angle X-ray scattering (SAXS) data. Each polymerization step of the coat proteins was assumed to be specified by a single equilibrium constant, and the equilibrium constant was evaluated by fitting the size and shape of the constituents observed by SAXS to those calculated from an assumed polymerization scheme. The logarithmic plots of the equilibrium constant against the inverse of temperature were fitted with a straight line at each buffer concentration and the thermodynamic quantities were evaluated from its intercept (yielding entropy) and slope (yielding enthalpy). The enthalpy and entropy values of TMV protein were found to be independent of buffer concentration, whereas those of CGMMV protein depended strongly on buffer concentration. In the limit, as ionic strength tends to infinity, both the enthalpy and entropy values of CGMMV protein approach those of TMV protein. The higher negative surface charge of CGMMV protein is considered to be responsible for the formation of stable single-layered disks, and for the slow polymerization process even at higher temperature and higher buffer concentrations.</div></front></TEI><istex><corpusName>oup</corpusName><keywords><teeft><json:string>cgmmv</json:string><json:string>cgmmv protein</json:string><json:string>molecular weight</json:string><json:string>lauffer</json:string><json:string>subunit</json:string><json:string>ionic strength</json:string><json:string>buffer concentration</json:string><json:string>sano</json:string><json:string>equilibrium constant</json:string><json:string>biochem</json:string><json:string>inoue</json:string><json:string>gyration</json:string><json:string>datum</json:string><json:string>entropy value</json:string><json:string>cgmmv protein disk</json:string><json:string>aggregation</json:string><json:string>sedimentation velocity</json:string><json:string>straight line</json:string><json:string>aggregation scheme</json:string><json:string>higher temperature</json:string><json:string>axial interaction</json:string><json:string>coat protein</json:string><json:string>axial direction</json:string><json:string>in diameter</json:string><json:string>thermodynamic parameter</json:string><json:string>thermodynamic analysis</json:string><json:string>major component</json:string><json:string>radial distribution function</json:string><json:string>previous paper</json:string><json:string>sax datum</json:string><json:string>guinier plot</json:string><json:string>cgmmv protein solution</json:string><json:string>enthalpy</json:string><json:string>protein</json:string><json:string>axial</json:string><json:string>initial slope</json:string><json:string>cgmmv protein aggregate</json:string><json:string>virus protein</json:string><json:string>simple equilibrium polymerization</json:string><json:string>sax intensity</json:string><json:string>weightaverage molecular weight</json:string><json:string>initial step</json:string><json:string>disk fragment</json:string><json:string>coat protein subunit</json:string><json:string>hollow disk</json:string><json:string>amino acid residue</json:string><json:string>phosphate buffer</json:string><json:string>amino acid sequence</json:string><json:string>protein solution</json:string><json:string>fiber diffraction</json:string><json:string>higher negative surface charge</json:string><json:string>laser light</json:string><json:string>condensation polymerization</json:string><json:string>single equilibrium constant</json:string><json:string>weight fraction</json:string><json:string>experimental value</json:string><json:string>secondary structure</json:string><json:string>water molecule</json:string><json:string>cucumber green mottle mosaic virus</json:string><json:string>doublelayered disk</json:string><json:string>protein disk</json:string><json:string>thermodynamic</json:string></teeft></keywords><author><json:item><name>Yoh Sano</name><affiliations><json:string>National Food Research Institute Tsukuba, Ibaraki 305</json:string></affiliations></json:item><json:item><name>Hideo Inoue</name><affiliations><json:string>Shimadzu Corporation Nakagyo-ku, Kyoto 604</json:string></affiliations></json:item><json:item><name>Kanji Kajiwara</name><affiliations><json:string>Faculty of Engineering and Design, Kyoto Institute of Technology Sakyo-ku, Kyoto 606</json:string></affiliations></json:item><json:item><name>Hiroshi Urakawa</name><affiliations><json:string>Faculty of Engineering and Design, Kyoto Institute of Technology Sakyo-ku, Kyoto 606</json:string></affiliations></json:item><json:item><name>Yuzuru Hiragi</name><affiliations><json:string>Institute for Chemical Research, Kyoto University Uji, Kyoto 611</json:string></affiliations></json:item></author><subject><json:item><value>cucumber green mottle mosaic virus protein</value></json:item><json:item><value>radius of gyration</value></json:item><json:item><value>small-angle X-ray scattering</value></json:item><json:item><value>tobacco masaic virus protein</value></json:item></subject><articleId><json:string>115.6.1058</json:string></articleId><arkIstex>ark:/67375/HXZ-2J964QTQ-V</arkIstex><language><json:string>unknown</json:string></language><originalGenre><json:string>research-article</json:string></originalGenre><abstract>The self-assembly process of cucumber green mottle mosaic virus (CGMMV) protein and tobacco mosaic virus (TMV) protein was examined by the thermodynamic analysis of small-angle X-ray scattering (SAXS) data. Each polymerization step of the coat proteins was assumed to be specified by a single equilibrium constant, and the equilibrium constant was evaluated by fitting the size and shape of the constituents observed by SAXS to those calculated from an assumed polymerization scheme. The logarithmic plots of the equilibrium constant against the inverse of temperature were fitted with a straight line at each buffer concentration and the thermodynamic quantities were evaluated from its intercept (yielding entropy) and slope (yielding enthalpy). The enthalpy and entropy values of TMV protein were found to be independent of buffer concentration, whereas those of CGMMV protein depended strongly on buffer concentration. In the limit, as ionic strength tends to infinity, both the enthalpy and entropy values of CGMMV protein approach those of TMV protein. The higher negative surface charge of CGMMV protein is considered to be responsible for the formation of stable single-layered disks, and for the slow polymerization process even at higher temperature and higher buffer concentrations.</abstract><qualityIndicators><score>6.559</score><pdfWordCount>4255</pdfWordCount><pdfCharCount>24663</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>6</pdfPageCount><pdfPageSize>598 x 783 pts</pdfPageSize><pdfWordsPerPage>709</pdfWordsPerPage><pdfText>true</pdfText><refBibsNative>false</refBibsNative><abstractWordCount>192</abstractWordCount><abstractCharCount>1293</abstractCharCount><keywordCount>4</keywordCount></qualityIndicators><title>Self-Assembling Process of Cylindrical Virus Coat Proteins as Observed by Synchrotron Small-Angle X-Ray Scattering</title><pmid><json:string>7982882</json:string></pmid><genre><json:string>research-article</json:string></genre><host><title>The Journal of Biochemistry</title><language><json:string>unknown</json:string></language><issn><json:string>0021-924X</json:string></issn><eissn><json:string>-</json:string></eissn><publisherId><json:string>jbchem</json:string></publisherId><volume>115</volume><issue>6</issue><pages><first>1058</first><last>1063</last></pages><genre><json:string>journal</json:string></genre><subject><json:item><value>Regular Papers</value></json:item></subject></host><namedEntities><unitex><date><json:string>21S</json:string><json:string>13S</json:string><json:string>17S</json:string><json:string>20S</json:string><json:string>1994</json:string></date><geogName></geogName><orgName><json:string>Kyoto Institute of Technology, Sakyo</json:string><json:string>Data Processing Center</json:string><json:string>Biochem</json:string><json:string>Institute for Chemical Research, Kyoto University, Uji, Kyoto</json:string><json:string>Ministry of Agriculture, Forestry, and Fisheries of Japan</json:string><json:string>National Laboratory for High Energy Physics, Tsukuba</json:string><json:string>National Food Research Institute, Tsukuba, Ibaraki</json:string><json:string>University of Tokyo</json:string><json:string>Shimadzu Corporation</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>The</json:string><json:string>Eiko Kurakami</json:string></persName><placeName><json:string>Kyoto</json:string><json:string>Japan</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Hiragi et al</json:string><json:string>Sturtevant et al.</json:string><json:string>Raghavendra et al.</json:string><json:string>Lauffer et al.</json:string><json:string>Hiragi et al.</json:string><json:string>Y. Sano et al.</json:string><json:string>Sturtevant et aL</json:string><json:string>Lobert et al.</json:string><json:string>Butler et al</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/HXZ-2J964QTQ-V</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - biochemistry & molecular biology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Molecular Biology</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Biochemistry</json:string><json:string>1 - Health Sciences</json:string><json:string>2 - Medicine</json:string><json:string>3 - General Medicine</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1994</publicationDate><copyrightDate>1994</copyrightDate><doi><json:string>10.1093/oxfordjournals.jbchem.a124457</json:string></doi><id>C5675519F6EAC4B43F8C17D3EB36E96F48E7525E</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/HXZ-2J964QTQ-V/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/HXZ-2J964QTQ-V/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/HXZ-2J964QTQ-V/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main">Self-Assembling Process of Cylindrical Virus Coat Proteins as Observed by Synchrotron Small-Angle X-Ray Scattering<ref type="fn" target="#fn1"><hi rend="superscript">1</hi></ref></title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Oxford University Press</publisher><availability><licence>© BY THE JOURNAL OF BIOCHEMISTRY</licence></availability><date type="Copyright" when="1994">1994</date><date type="published">1994</date></publicationStmt><notesStmt><note type="content-type" source="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="publication-type" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="article"><analytic><title level="a" type="main">Self-Assembling Process of Cylindrical Virus Coat Proteins as Observed by Synchrotron Small-Angle X-Ray Scattering<ref type="fn" target="#fn1"><hi rend="superscript">1</hi></ref></title><author xml:id="author-0000"><persName><surname>Sano</surname><forename type="first">Yoh</forename></persName><affiliation><orgName type="institution">National Food Research Institute</orgName><address><addrLine>Tsukuba, Ibaraki 305</addrLine></address></affiliation></author><author xml:id="author-0001"><persName><surname>Inoue</surname><forename type="first">Hideo</forename></persName><affiliation><orgName type="institution">Shimadzu Corporation</orgName><address><addrLine>Nakagyo-ku, Kyoto 604</addrLine></address></affiliation></author><author xml:id="author-0002"><persName><surname>Kajiwara</surname><forename type="first">Kanji</forename></persName><affiliation><orgName type="institution">Faculty of Engineering and Design, Kyoto Institute of Technology</orgName><address><addrLine>Sakyo-ku, Kyoto 606</addrLine></address></affiliation></author><author xml:id="author-0003"><persName><surname>Urakawa</surname><forename type="first">Hiroshi</forename></persName><affiliation><orgName type="institution">Faculty of Engineering and Design, Kyoto Institute of Technology</orgName><address><addrLine>Sakyo-ku, Kyoto 606</addrLine></address></affiliation></author><author xml:id="author-0004"><persName><surname>Hiragi</surname><forename type="first">Yuzuru</forename></persName><affiliation><orgName type="institution">Institute for Chemical Research, Kyoto University</orgName><address><addrLine>Uji, Kyoto 611</addrLine></address></affiliation></author><idno type="istex">C5675519F6EAC4B43F8C17D3EB36E96F48E7525E</idno><idno type="ark">ark:/67375/HXZ-2J964QTQ-V</idno><idno type="publisher-id">115.6.1058</idno><idno type="DOI">10.1093/oxfordjournals.jbchem.a124457</idno></analytic><monogr><title level="j" type="main">The Journal of Biochemistry</title><idno type="hwp">jbiochem</idno><idno type="publisher-id">jbchem</idno><idno type="pmc">jbiochem</idno><idno type="eISSN">-</idno><idno type="pISSN">0021-924X</idno><imprint><publisher>Oxford University Press</publisher><date type="published">1994</date><biblScope unit="vol">115</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="1058">1058</biblScope><biblScope unit="page" to="1063">1063</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><encodingDesc><schemaRef type="ODD" url="https://xml-schema.delivery.istex.fr/tei-istex.odd"></schemaRef><appInfo><application ident="pub2tei" version="1.0.41" when="2020-04-06"><label>pub2TEI-ISTEX</label><desc>A set of style sheets for converting XML documents encoded in various scientific publisher formats into a common TEI format.
<ref target="http://www.tei-c.org/">We use TEI</ref></desc></application></appInfo></encodingDesc><profileDesc><abstract><p>The self-assembly process of cucumber green mottle mosaic virus (CGMMV) protein and tobacco mosaic virus (TMV) protein was examined by the thermodynamic analysis of small-angle X-ray scattering (SAXS) data. Each polymerization step of the coat proteins was assumed to be specified by a single equilibrium constant, and the equilibrium constant was evaluated by fitting the size and shape of the constituents observed by SAXS to those calculated from an assumed polymerization scheme. The logarithmic plots of the equilibrium constant against the inverse of temperature were fitted with a straight line at each buffer concentration and the thermodynamic quantities were evaluated from its intercept (yielding entropy) and slope (yielding enthalpy). The enthalpy and entropy values of TMV protein were found to be independent of buffer concentration, whereas those of CGMMV protein depended strongly on buffer concentration. In the limit, as ionic strength tends to infinity, both the enthalpy and entropy values of CGMMV protein approach those of TMV protein. The higher negative surface charge of CGMMV protein is considered to be responsible for the formation of stable single-layered disks, and for the slow polymerization process even at higher temperature and higher buffer concentrations.</p></abstract><textClass ana="subject"><keywords scheme="subject"><term>Regular Papers</term></keywords></textClass><textClass ana="keyword"><keywords><term>cucumber green mottle mosaic virus protein</term><term>radius of gyration</term><term>small-angle X-ray scattering</term><term>tobacco masaic virus protein</term></keywords></textClass><langUsage><language ident="EN"></language></langUsage></profileDesc><revisionDesc><change when="2020-04-06" who="#istex" xml:id="pub2tei">formatting</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/HXZ-2J964QTQ-V/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="corpus oup, element #text not found" wicri:toSee="no header"><istex:docType PUBLIC="-//NLM//DTD Journal Publishing DTD v2.3 20070202//EN" URI="journalpublishing.dtd" name="istex:docType"></istex:docType><istex:document><article article-type="research-article">
<front>
<journal-meta>
<journal-id journal-id-type="hwp">jbiochem</journal-id>
<journal-id journal-id-type="publisher-id">jbchem</journal-id>
<journal-id journal-id-type="pmc">jbiochem</journal-id>
<journal-title>The Journal of Biochemistry</journal-title>
<issn pub-type="epub">-</issn>
<issn pub-type="ppub">0021-924X</issn>
<publisher>
<publisher-name>Oxford University Press</publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id pub-id-type="publisher-id">115.6.1058</article-id>
<article-id pub-id-type="doi">10.1093/oxfordjournals.jbchem.a124457</article-id>
<article-categories>
<subj-group>
<subject>Regular Papers</subject>
</subj-group>
</article-categories>
<title-group>
<article-title>Self-Assembling Process of Cylindrical Virus Coat Proteins as Observed by Synchrotron Small-Angle X-Ray Scattering<xref ref-type="fn" rid="fn1"><sup>1</sup></xref></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name><surname>Sano</surname><given-names>Yoh</given-names></name><xref ref-type="aff" rid="au1"><sup>*</sup></xref>
</contrib>
<contrib contrib-type="author">
<name><surname>Inoue</surname><given-names>Hideo</given-names></name><xref ref-type="aff" rid="au2"><sup>**</sup></xref>
</contrib>
<contrib contrib-type="author">
<name><surname>Kajiwara</surname><given-names>Kanji</given-names></name><xref ref-type="aff" rid="au3"><sup>***</sup></xref>
</contrib>
<contrib contrib-type="author">
<name><surname>Urakawa</surname><given-names>Hiroshi</given-names></name><xref ref-type="aff" rid="au3"><sup>***</sup></xref>
</contrib>
<contrib contrib-type="author">
<name><surname>Hiragi</surname><given-names>Yuzuru</given-names></name><xref ref-type="aff" rid="au4"><sup>****</sup></xref>
</contrib>
<aff id="au1"><sup>*</sup><institution>National Food Research Institute</institution> <addr-line>Tsukuba, Ibaraki 305</addr-line></aff>
<aff id="au2"><sup>**</sup><institution>Shimadzu Corporation</institution> <addr-line>Nakagyo-ku, Kyoto 604</addr-line></aff>
<aff id="au3"><sup>***</sup><institution>Faculty of Engineering and Design, Kyoto Institute of Technology</institution> <addr-line>Sakyo-ku, Kyoto 606</addr-line></aff>
<aff id="au4"><sup>****</sup><institution>Institute for Chemical Research, Kyoto University</institution> <addr-line>Uji, Kyoto 611</addr-line></aff>
</contrib-group>
<author-notes>
<fn id="fn1"><p><sup>1</sup>This work was supported in part by a Grant-in-Aid (Bio Media Program) from the Ministry of Agriculture, Forestry, and Fisheries of Japan (BMP 94-VI-5-2).</p></fn>
</author-notes>
<pub-date pub-type="ppub">
<month>6</month>
<year>1994</year>
</pub-date>
<volume>115</volume>
<issue>6</issue>
<fpage>1058</fpage>
<lpage>1063</lpage>
<history>
<date date-type="received">
<day>26</day>
<month>11</month>
<year>1993</year>
</date>
</history>
<copyright-statement>© BY THE JOURNAL OF BIOCHEMISTRY</copyright-statement>
<copyright-year>1994</copyright-year>
<abstract>
<p>The self-assembly process of cucumber green mottle mosaic virus (CGMMV) protein and tobacco mosaic virus (TMV) protein was examined by the thermodynamic analysis of small-angle X-ray scattering (SAXS) data. Each polymerization step of the coat proteins was assumed to be specified by a single equilibrium constant, and the equilibrium constant was evaluated by fitting the size and shape of the constituents observed by SAXS to those calculated from an assumed polymerization scheme. The logarithmic plots of the equilibrium constant against the inverse of temperature were fitted with a straight line at each buffer concentration and the thermodynamic quantities were evaluated from its intercept (yielding entropy) and slope (yielding enthalpy). The enthalpy and entropy values of TMV protein were found to be independent of buffer concentration, whereas those of CGMMV protein depended strongly on buffer concentration. In the limit, as ionic strength tends to infinity, both the enthalpy and entropy values of CGMMV protein approach those of TMV protein. The higher negative surface charge of CGMMV protein is considered to be responsible for the formation of stable single-layered disks, and for the slow polymerization process even at higher temperature and higher buffer concentrations.</p>
</abstract>
<kwd-group>
<kwd>cucumber green mottle mosaic virus protein</kwd>
<kwd>radius of gyration</kwd>
<kwd>small-angle X-ray scattering</kwd>
<kwd>tobacco masaic virus protein</kwd>
</kwd-group>
</article-meta>
</front>
</article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Self-Assembling Process of Cylindrical Virus Coat Proteins as Observed by Synchrotron Small-Angle X-Ray Scattering</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Self-Assembling Process of Cylindrical Virus Coat Proteins as Observed by Synchrotron Small-Angle X-Ray Scattering1</title></titleInfo><name type="personal"><namePart type="given">Yoh</namePart><namePart type="family">Sano</namePart><affiliation>National Food Research Institute Tsukuba, Ibaraki 305</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Hideo</namePart><namePart type="family">Inoue</namePart><affiliation>Shimadzu Corporation Nakagyo-ku, Kyoto 604</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Kanji</namePart><namePart type="family">Kajiwara</namePart><affiliation>Faculty of Engineering and Design, Kyoto Institute of Technology Sakyo-ku, Kyoto 606</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Hiroshi</namePart><namePart type="family">Urakawa</namePart><affiliation>Faculty of Engineering and Design, Kyoto Institute of Technology Sakyo-ku, Kyoto 606</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Yuzuru</namePart><namePart type="family">Hiragi</namePart><affiliation>Institute for Chemical Research, Kyoto University Uji, Kyoto 611</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="research-article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>Oxford University Press</publisher><dateIssued encoding="w3cdtf">1994-06</dateIssued><copyrightDate encoding="w3cdtf">1994</copyrightDate></originInfo><abstract>The self-assembly process of cucumber green mottle mosaic virus (CGMMV) protein and tobacco mosaic virus (TMV) protein was examined by the thermodynamic analysis of small-angle X-ray scattering (SAXS) data. Each polymerization step of the coat proteins was assumed to be specified by a single equilibrium constant, and the equilibrium constant was evaluated by fitting the size and shape of the constituents observed by SAXS to those calculated from an assumed polymerization scheme. The logarithmic plots of the equilibrium constant against the inverse of temperature were fitted with a straight line at each buffer concentration and the thermodynamic quantities were evaluated from its intercept (yielding entropy) and slope (yielding enthalpy). The enthalpy and entropy values of TMV protein were found to be independent of buffer concentration, whereas those of CGMMV protein depended strongly on buffer concentration. In the limit, as ionic strength tends to infinity, both the enthalpy and entropy values of CGMMV protein approach those of TMV protein. The higher negative surface charge of CGMMV protein is considered to be responsible for the formation of stable single-layered disks, and for the slow polymerization process even at higher temperature and higher buffer concentrations.</abstract><note type="footnotes">1This work was supported in part by a Grant-in-Aid (Bio Media Program) from the Ministry of Agriculture, Forestry, and Fisheries of Japan (BMP 94-VI-5-2).</note><subject><genre>keywords</genre><topic>cucumber green mottle mosaic virus protein</topic><topic>radius of gyration</topic><topic>small-angle X-ray scattering</topic><topic>tobacco masaic virus protein</topic></subject><relatedItem type="host"><titleInfo><title>The Journal of Biochemistry</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><subject><topic>Regular Papers</topic></subject><identifier type="ISSN">0021-924X</identifier><identifier type="eISSN">-</identifier><identifier type="PublisherID">jbchem</identifier><identifier type="PublisherID-hwp">jbiochem</identifier><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>115</number></detail><detail type="issue"><caption>no.</caption><number>6</number></detail><extent unit="pages"><start>1058</start><end>1063</end></extent></part></relatedItem><identifier type="istex">C5675519F6EAC4B43F8C17D3EB36E96F48E7525E</identifier><identifier type="ark">ark:/67375/HXZ-2J964QTQ-V</identifier><identifier type="DOI">10.1093/oxfordjournals.jbchem.a124457</identifier><identifier type="ArticleID">115.6.1058</identifier><accessCondition type="use and reproduction" contentType="copyright">© BY THE JOURNAL OF BIOCHEMISTRY</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-GTWS0RDP-M">oup</recordContentSource><recordOrigin>Converted from (version 1.2.10) to MODS version 3.6.</recordOrigin><recordCreationDate encoding="w3cdtf">2020-04-16</recordCreationDate></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/HXZ-2J964QTQ-V/record.json</uri></json:item></metadata><annexes><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/HXZ-2J964QTQ-V/annexes.pdf</uri></json:item></annexes><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Istex/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000873 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Istex/Corpus/biblio.hfd -nk 000873 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= MersV1
|flux= Istex
|étape= Corpus
|type= RBID
|clé= ISTEX:C5675519F6EAC4B43F8C17D3EB36E96F48E7525E
|texte= Self-Assembling Process of Cylindrical Virus Coat Proteins as Observed by Synchrotron Small-Angle X-Ray Scattering
}}
| This area was generated with Dilib version V0.6.33. |  |