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.
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DOI: 10.1093/oxfordjournals.jbchem.a124457
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<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>
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<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>
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<mods version="3.6"><titleInfo><title>Self-Assembling Process of Cylindrical Virus Coat Proteins as Observed by Synchrotron Small-Angle X-Ray Scattering</title>
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<titleInfo type="alternative" contentType="CDATA"><title>Self-Assembling Process of Cylindrical Virus Coat Proteins as Observed by Synchrotron Small-Angle X-Ray Scattering1</title>
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<name type="personal"><namePart type="given">Yoh</namePart>
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<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>
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