Size distribution of protein polymers
Identifieur interne : 000199 ( Istex/Corpus ); précédent : 000198; suivant : 000200Size distribution of protein polymers
Auteurs : Fumio OosawaSource :
- Journal of Theoretical Biology [ 0022-5193 ] ; 1970.
English descriptors
- Teeft :
- Actin, Actin polymers, Asakura, Average degree, Average length, Bacterial flagellin, Biol, Biological systems, Casper, Critical concentration, Crystallization, Depolymerization, Experimental data, Final equilibrium, Final stage, Flagellin, Free energy, Globular, Globular protein molecules, Helical, Kasai, Kawamura, Kinetic constants, Macroscopic polymers, Maruyama, Molec, Monomer, Monomer concentration, Neighbouring, Neighbouring monomers, Number concentration, Oosawa, Oosawa higashi, Oosawa kasai, Poisson distribution, Polymer, Polymer size, Polymerization, Polymerization equilibrium, Present case, Present theory, Previous case, Protein molecules, Protein polymers, Relative deviation, Relaxation time, Reversible polymerization, Second term, Short polymers, Size distribution, Small polymers, Sonic vibration, Spontaneous nucleation, Total concentration, Total number, Total number concentration, True equilibrium, Tubular polymers, Various conditions.
Abstract
Abstract: Theoretical analyses were made on the size distribution of tubular or helical polymers of globular protein molecules in the reversible polymerization. In the true final equilibrium, polymerization approximates to a kind of crystallization and the average degree of polymerization becomes very large; nevertheless, the size distribution is of a simple exponential type, the same as found in macromolecular chemistry (Flory, 1953). Even when spontaneous nucleation is inhibited and the number of polymers is given, the final distribution must tend towards the exponential type. Free energy due to deviation of the size distribution from the true equilibrium was calculated. It is very much smaller than the main free energy coming from the monomer-polymer equilibrium. Kinetics showed that polymerization having characteristics of crystallization usually consists of three stages—nucleation, growth and redistribution of polymer size. In the first and second stages where the rate of depolymerization is negligible, the concentration of monomers approaches closely to the equilibrium value. In the third stage, where both polymerization and depolymerization take place nearly at the same rate, the size distribution is slowly transformed into the exponential type. The relaxation time for such redistribution was estimated as a function of rate constants and the average degree of polymerization under various conditions. All of the theoretical results are quantitatively in good agreement with experimental data on polymerization of globular proteins such as actin and flagellin. Brief analyses were added on the size distribution of two-dimensional membraneous polymers and distorted polymers.
Url:
DOI: 10.1016/0022-5193(70)90129-3
Links to Exploration step
ISTEX:A691845732EF9D819113F3867C2F1BC5D5E294E0Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Size distribution of protein polymers</title><author><name sortKey="Oosawa, Fumio" sort="Oosawa, Fumio" uniqKey="Oosawa F" first="Fumio" last="Oosawa">Fumio Oosawa</name><affiliation><mods:affiliation>Institute of Molecular Biology, Faculty of Science, Nagoya University, Nagoya, Japan</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:A691845732EF9D819113F3867C2F1BC5D5E294E0</idno><date when="1970" year="1970">1970</date><idno type="doi">10.1016/0022-5193(70)90129-3</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-QMVGRQBZ-S/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000199</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000199</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Size distribution of protein polymers</title><author><name sortKey="Oosawa, Fumio" sort="Oosawa, Fumio" uniqKey="Oosawa F" first="Fumio" last="Oosawa">Fumio Oosawa</name><affiliation><mods:affiliation>Institute of Molecular Biology, Faculty of Science, Nagoya University, Nagoya, Japan</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Theoretical Biology</title><title level="j" type="abbrev">YJTBI</title><idno type="ISSN">0022-5193</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1970">1970</date><biblScope unit="volume">27</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="69">69</biblScope><biblScope unit="page" to="86">86</biblScope></imprint><idno type="ISSN">0022-5193</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0022-5193</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Actin</term><term>Actin polymers</term><term>Asakura</term><term>Average degree</term><term>Average length</term><term>Bacterial flagellin</term><term>Biol</term><term>Biological systems</term><term>Casper</term><term>Critical concentration</term><term>Crystallization</term><term>Depolymerization</term><term>Experimental data</term><term>Final equilibrium</term><term>Final stage</term><term>Flagellin</term><term>Free energy</term><term>Globular</term><term>Globular protein molecules</term><term>Helical</term><term>Kasai</term><term>Kawamura</term><term>Kinetic constants</term><term>Macroscopic polymers</term><term>Maruyama</term><term>Molec</term><term>Monomer</term><term>Monomer concentration</term><term>Neighbouring</term><term>Neighbouring monomers</term><term>Number concentration</term><term>Oosawa</term><term>Oosawa higashi</term><term>Oosawa kasai</term><term>Poisson distribution</term><term>Polymer</term><term>Polymer size</term><term>Polymerization</term><term>Polymerization equilibrium</term><term>Present case</term><term>Present theory</term><term>Previous case</term><term>Protein molecules</term><term>Protein polymers</term><term>Relative deviation</term><term>Relaxation time</term><term>Reversible polymerization</term><term>Second term</term><term>Short polymers</term><term>Size distribution</term><term>Small polymers</term><term>Sonic vibration</term><term>Spontaneous nucleation</term><term>Total concentration</term><term>Total number</term><term>Total number concentration</term><term>True equilibrium</term><term>Tubular polymers</term><term>Various conditions</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Theoretical analyses were made on the size distribution of tubular or helical polymers of globular protein molecules in the reversible polymerization. In the true final equilibrium, polymerization approximates to a kind of crystallization and the average degree of polymerization becomes very large; nevertheless, the size distribution is of a simple exponential type, the same as found in macromolecular chemistry (Flory, 1953). Even when spontaneous nucleation is inhibited and the number of polymers is given, the final distribution must tend towards the exponential type. Free energy due to deviation of the size distribution from the true equilibrium was calculated. It is very much smaller than the main free energy coming from the monomer-polymer equilibrium. Kinetics showed that polymerization having characteristics of crystallization usually consists of three stages—nucleation, growth and redistribution of polymer size. In the first and second stages where the rate of depolymerization is negligible, the concentration of monomers approaches closely to the equilibrium value. In the third stage, where both polymerization and depolymerization take place nearly at the same rate, the size distribution is slowly transformed into the exponential type. The relaxation time for such redistribution was estimated as a function of rate constants and the average degree of polymerization under various conditions. All of the theoretical results are quantitatively in good agreement with experimental data on polymerization of globular proteins such as actin and flagellin. Brief analyses were added on the size distribution of two-dimensional membraneous polymers and distorted polymers.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>polymer</json:string><json:string>size distribution</json:string><json:string>oosawa</json:string><json:string>asakura</json:string><json:string>monomer</json:string><json:string>free energy</json:string><json:string>number concentration</json:string><json:string>biol</json:string><json:string>actin</json:string><json:string>flagellin</json:string><json:string>helical</json:string><json:string>depolymerization</json:string><json:string>critical concentration</json:string><json:string>true equilibrium</json:string><json:string>total number</json:string><json:string>neighbouring</json:string><json:string>average degree</json:string><json:string>globular</json:string><json:string>tubular polymers</json:string><json:string>casper</json:string><json:string>molec</json:string><json:string>monomer concentration</json:string><json:string>protein polymers</json:string><json:string>kawamura</json:string><json:string>maruyama</json:string><json:string>oosawa kasai</json:string><json:string>total concentration</json:string><json:string>relaxation time</json:string><json:string>poisson distribution</json:string><json:string>average length</json:string><json:string>globular protein molecules</json:string><json:string>previous case</json:string><json:string>oosawa higashi</json:string><json:string>neighbouring monomers</json:string><json:string>polymerization</json:string><json:string>spontaneous nucleation</json:string><json:string>final stage</json:string><json:string>polymerization equilibrium</json:string><json:string>second term</json:string><json:string>biological systems</json:string><json:string>kinetic constants</json:string><json:string>sonic vibration</json:string><json:string>polymer size</json:string><json:string>kasai</json:string><json:string>experimental data</json:string><json:string>bacterial flagellin</json:string><json:string>total number concentration</json:string><json:string>various conditions</json:string><json:string>present case</json:string><json:string>present theory</json:string><json:string>relative deviation</json:string><json:string>small polymers</json:string><json:string>protein molecules</json:string><json:string>reversible polymerization</json:string><json:string>final equilibrium</json:string><json:string>macroscopic polymers</json:string><json:string>short polymers</json:string><json:string>actin polymers</json:string><json:string>crystallization</json:string></teeft></keywords><author><json:item><name>Fumio Oosawa</name><affiliations><json:string>Institute of Molecular Biology, Faculty of Science, Nagoya University, Nagoya, Japan</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-QMVGRQBZ-S</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Theoretical analyses were made on the size distribution of tubular or helical polymers of globular protein molecules in the reversible polymerization. In the true final equilibrium, polymerization approximates to a kind of crystallization and the average degree of polymerization becomes very large; nevertheless, the size distribution is of a simple exponential type, the same as found in macromolecular chemistry (Flory, 1953). Even when spontaneous nucleation is inhibited and the number of polymers is given, the final distribution must tend towards the exponential type. Free energy due to deviation of the size distribution from the true equilibrium was calculated. It is very much smaller than the main free energy coming from the monomer-polymer equilibrium. Kinetics showed that polymerization having characteristics of crystallization usually consists of three stages—nucleation, growth and redistribution of polymer size. In the first and second stages where the rate of depolymerization is negligible, the concentration of monomers approaches closely to the equilibrium value. In the third stage, where both polymerization and depolymerization take place nearly at the same rate, the size distribution is slowly transformed into the exponential type. The relaxation time for such redistribution was estimated as a function of rate constants and the average degree of polymerization under various conditions. All of the theoretical results are quantitatively in good agreement with experimental data on polymerization of globular proteins such as actin and flagellin. 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In the true final equilibrium, polymerization approximates to a kind of crystallization and the average degree of polymerization becomes very large; nevertheless, the size distribution is of a simple exponential type, the same as found in macromolecular chemistry (Flory, 1953). Even when spontaneous nucleation is inhibited and the number of polymers is given, the final distribution must tend towards the exponential type. Free energy due to deviation of the size distribution from the true equilibrium was calculated. It is very much smaller than the main free energy coming from the monomer-polymer equilibrium. Kinetics showed that polymerization having characteristics of crystallization usually consists of three stages—nucleation, growth and redistribution of polymer size. In the first and second stages where the rate of depolymerization is negligible, the concentration of monomers approaches closely to the equilibrium value. In the third stage, where both polymerization and depolymerization take place nearly at the same rate, the size distribution is slowly transformed into the exponential type. The relaxation time for such redistribution was estimated as a function of rate constants and the average degree of polymerization under various conditions. All of the theoretical results are quantitatively in good agreement with experimental data on polymerization of globular proteins such as actin and flagellin. Brief analyses were added on the size distribution of two-dimensional membraneous polymers and distorted polymers.</p></abstract></profileDesc><revisionDesc><change when="1969-10-20">Modified</change><change when="1970">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-QMVGRQBZ-S/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>YJTBI</jid><aid>70901293</aid><ce:pii>0022-5193(70)90129-3</ce:pii><ce:doi>10.1016/0022-5193(70)90129-3</ce:doi><ce:copyright type="unknown" year="1970"></ce:copyright></item-info><head><ce:title>Size distribution of protein polymers</ce:title><ce:author-group><ce:author><ce:given-name>Fumio</ce:given-name><ce:surname>Oosawa</ce:surname></ce:author><ce:affiliation><ce:textfn>Institute of Molecular Biology, Faculty of Science, Nagoya University, Nagoya, Japan</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="15" month="8" year="1969"></ce:date-received><ce:date-revised day="20" month="10" year="1969"></ce:date-revised><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Theoretical analyses were made on the size distribution of tubular or helical polymers of globular protein molecules in the reversible polymerization. In the true final equilibrium, polymerization approximates to a kind of crystallization and the average degree of polymerization becomes very large; nevertheless, the size distribution is of a simple exponential type, the same as found in macromolecular chemistry (<ce:cross-ref refid="BIB8">Flory, 1953</ce:cross-ref>). Even when spontaneous nucleation is inhibited and the number of polymers is given, the final distribution must tend towards the exponential type. Free energy due to deviation of the size distribution from the true equilibrium was calculated. It is very much smaller than the main free energy coming from the monomer-polymer equilibrium.</ce:simple-para><ce:simple-para>Kinetics showed that polymerization having characteristics of crystallization usually consists of three stages—nucleation, growth and redistribution of polymer size. In the first and second stages where the rate of depolymerization is negligible, the concentration of monomers approaches closely to the equilibrium value. In the third stage, where both polymerization and depolymerization take place nearly at the same rate, the size distribution is slowly transformed into the exponential type. The relaxation time for such redistribution was estimated as a function of rate constants and the average degree of polymerization under various conditions.</ce:simple-para><ce:simple-para>All of the theoretical results are quantitatively in good agreement with experimental data on polymerization of globular proteins such as actin and flagellin. Brief analyses were added on the size distribution of two-dimensional membraneous polymers and distorted polymers.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Size distribution of protein polymers</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Size distribution of protein polymers</title></titleInfo><name type="personal"><namePart type="given">Fumio</namePart><namePart type="family">Oosawa</namePart><affiliation>Institute of Molecular Biology, Faculty of Science, Nagoya University, Nagoya, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length 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>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1970</dateIssued><dateModified encoding="w3cdtf">1969-10-20</dateModified><copyrightDate encoding="w3cdtf">1970</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Theoretical analyses were made on the size distribution of tubular or helical polymers of globular protein molecules in the reversible polymerization. In the true final equilibrium, polymerization approximates to a kind of crystallization and the average degree of polymerization becomes very large; nevertheless, the size distribution is of a simple exponential type, the same as found in macromolecular chemistry (Flory, 1953). Even when spontaneous nucleation is inhibited and the number of polymers is given, the final distribution must tend towards the exponential type. Free energy due to deviation of the size distribution from the true equilibrium was calculated. It is very much smaller than the main free energy coming from the monomer-polymer equilibrium. Kinetics showed that polymerization having characteristics of crystallization usually consists of three stages—nucleation, growth and redistribution of polymer size. In the first and second stages where the rate of depolymerization is negligible, the concentration of monomers approaches closely to the equilibrium value. In the third stage, where both polymerization and depolymerization take place nearly at the same rate, the size distribution is slowly transformed into the exponential type. The relaxation time for such redistribution was estimated as a function of rate constants and the average degree of polymerization under various conditions. All of the theoretical results are quantitatively in good agreement with experimental data on polymerization of globular proteins such as actin and flagellin. 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