Model for amorphous aggregation processes.
Identifieur interne : 000314 ( Main/Exploration ); précédent : 000313; suivant : 000315Model for amorphous aggregation processes.
Auteurs : Samuel D. Stranks [Australie] ; Heath Ecroyd ; Steven Van Sluyter ; Elizabeth J. Waters ; John A. Carver ; Lorenz Von SmekalSource :
- Physical review. E, Statistical, nonlinear, and soft matter physics [ 1550-2376 ] ; 2009.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Complexes multiprotéiques, Protéines.
- ultrastructure : Complexes multiprotéiques, Protéines.
- Dimérisation, Modèles chimiques, Modèles moléculaires, Simulation numérique.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Multiprotein Complexes, Proteins.
- chemical , ultrastructure : Multiprotein Complexes, Proteins.
- Computer Simulation, Dimerization, Models, Chemical, Models, Molecular.
Abstract
The amorphous aggregation of proteins is associated with many phenomena, ranging from the formation of protein wine haze to the development of cataract in the eye lens and the precipitation of recombinant proteins during their expression and purification. While much literature exists describing models for linear protein aggregation, such as amyloid fibril formation, there are few reports of models which address amorphous aggregation. Here, we propose a model to describe the amorphous aggregation of proteins which is also more widely applicable to other situations where a similar process occurs, such as in the formation of colloids and nanoclusters. As first applications of the model, we have tested it against experimental turbidimetry data of three proteins relevant to the wine industry and biochemistry, namely, thaumatin, a thaumatinlike protein, and alpha -lactalbumin. The model is very robust and describes amorphous experimental data to a high degree of accuracy. Details about the aggregation process, such as shape parameters of the aggregates and rate constants, can also be extracted.
DOI: 10.1103/PhysRevE.80.051907
PubMed: 20365006
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Stranks</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry and Physics, The University of Adelaide, South Australia 5005, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Chemistry and Physics, The University of Adelaide, South Australia 5005</wicri:regionArea><wicri:noRegion>South Australia 5005</wicri:noRegion></affiliation></author><author><name sortKey="Ecroyd, Heath" sort="Ecroyd, Heath" uniqKey="Ecroyd H" first="Heath" last="Ecroyd">Heath Ecroyd</name></author><author><name sortKey="Van Sluyter, Steven" sort="Van Sluyter, Steven" uniqKey="Van Sluyter S" first="Steven" last="Van Sluyter">Steven Van Sluyter</name></author><author><name sortKey="Waters, Elizabeth J" sort="Waters, Elizabeth J" uniqKey="Waters E" first="Elizabeth J" last="Waters">Elizabeth J. Waters</name></author><author><name sortKey="Carver, John A" sort="Carver, John A" uniqKey="Carver J" first="John A" last="Carver">John A. Carver</name></author><author><name sortKey="Von Smekal, Lorenz" sort="Von Smekal, Lorenz" uniqKey="Von Smekal L" first="Lorenz" last="Von Smekal">Lorenz Von Smekal</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:20365006</idno><idno type="pmid">20365006</idno><idno type="doi">10.1103/PhysRevE.80.051907</idno><idno type="wicri:Area/Main/Corpus">000297</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000297</idno><idno type="wicri:Area/Main/Curation">000297</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000297</idno><idno type="wicri:Area/Main/Exploration">000297</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Model for amorphous aggregation processes.</title><author><name sortKey="Stranks, Samuel D" sort="Stranks, Samuel D" uniqKey="Stranks S" first="Samuel D" last="Stranks">Samuel D. 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Carver</name></author><author><name sortKey="Von Smekal, Lorenz" sort="Von Smekal, Lorenz" uniqKey="Von Smekal L" first="Lorenz" last="Von Smekal">Lorenz Von Smekal</name></author></analytic><series><title level="j">Physical review. E, Statistical, nonlinear, and soft matter physics</title><idno type="eISSN">1550-2376</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Computer Simulation (MeSH)</term><term>Dimerization (MeSH)</term><term>Models, Chemical (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Multiprotein Complexes (chemistry)</term><term>Multiprotein Complexes (ultrastructure)</term><term>Proteins (chemistry)</term><term>Proteins (ultrastructure)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Complexes multiprotéiques (composition chimique)</term><term>Complexes multiprotéiques (ultrastructure)</term><term>Dimérisation (MeSH)</term><term>Modèles chimiques (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Protéines (composition chimique)</term><term>Protéines (ultrastructure)</term><term>Simulation numérique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Multiprotein Complexes</term><term>Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Multiprotein Complexes</term><term>Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Complexes multiprotéiques</term><term>Protéines</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Complexes multiprotéiques</term><term>Protéines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Computer Simulation</term><term>Dimerization</term><term>Models, Chemical</term><term>Models, Molecular</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Dimérisation</term><term>Modèles chimiques</term><term>Modèles moléculaires</term><term>Simulation numérique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The amorphous aggregation of proteins is associated with many phenomena, ranging from the formation of protein wine haze to the development of cataract in the eye lens and the precipitation of recombinant proteins during their expression and purification. While much literature exists describing models for linear protein aggregation, such as amyloid fibril formation, there are few reports of models which address amorphous aggregation. Here, we propose a model to describe the amorphous aggregation of proteins which is also more widely applicable to other situations where a similar process occurs, such as in the formation of colloids and nanoclusters. As first applications of the model, we have tested it against experimental turbidimetry data of three proteins relevant to the wine industry and biochemistry, namely, thaumatin, a thaumatinlike protein, and alpha -lactalbumin. The model is very robust and describes amorphous experimental data to a high degree of accuracy. Details about the aggregation process, such as shape parameters of the aggregates and rate constants, can also be extracted.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20365006</PMID><DateCompleted><Year>2010</Year><Month>07</Month><Day>14</Day></DateCompleted><DateRevised><Year>2010</Year><Month>04</Month><Day>06</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1550-2376</ISSN><JournalIssue CitedMedium="Internet"><Volume>80</Volume><Issue>5 Pt 1</Issue><PubDate><Year>2009</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Physical review. E, Statistical, nonlinear, and soft matter physics</Title><ISOAbbreviation>Phys Rev E Stat Nonlin Soft Matter Phys</ISOAbbreviation></Journal><ArticleTitle>Model for amorphous aggregation processes.</ArticleTitle><Pagination><MedlinePgn>051907</MedlinePgn></Pagination><Abstract><AbstractText>The amorphous aggregation of proteins is associated with many phenomena, ranging from the formation of protein wine haze to the development of cataract in the eye lens and the precipitation of recombinant proteins during their expression and purification. While much literature exists describing models for linear protein aggregation, such as amyloid fibril formation, there are few reports of models which address amorphous aggregation. Here, we propose a model to describe the amorphous aggregation of proteins which is also more widely applicable to other situations where a similar process occurs, such as in the formation of colloids and nanoclusters. As first applications of the model, we have tested it against experimental turbidimetry data of three proteins relevant to the wine industry and biochemistry, namely, thaumatin, a thaumatinlike protein, and alpha -lactalbumin. The model is very robust and describes amorphous experimental data to a high degree of accuracy. Details about the aggregation process, such as shape parameters of the aggregates and rate constants, can also be extracted.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Stranks</LastName><ForeName>Samuel D</ForeName><Initials>SD</Initials><AffiliationInfo><Affiliation>School of Chemistry and Physics, The University of Adelaide, South Australia 5005, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ecroyd</LastName><ForeName>Heath</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Van Sluyter</LastName><ForeName>Steven</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Waters</LastName><ForeName>Elizabeth J</ForeName><Initials>EJ</Initials></Author><Author ValidYN="Y"><LastName>Carver</LastName><ForeName>John A</ForeName><Initials>JA</Initials></Author><Author ValidYN="Y"><LastName>von Smekal</LastName><ForeName>Lorenz</ForeName><Initials>L</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2009</Year><Month>11</Month><Day>09</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Phys Rev E Stat Nonlin Soft Matter Phys</MedlineTA><NlmUniqueID>101136452</NlmUniqueID><ISSNLinking>1539-3755</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D046912">Multiprotein Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003198" MajorTopicYN="N">Computer Simulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008956" MajorTopicYN="Y">Models, Chemical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="Y">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046912" MajorTopicYN="N">Multiprotein Complexes</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000648" MajorTopicYN="Y">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000648" MajorTopicYN="Y">ultrastructure</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2009</Year><Month>01</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2010</Year><Month>4</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2010</Year><Month>4</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>7</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20365006</ArticleId><ArticleId IdType="doi">10.1103/PhysRevE.80.051907</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li></country></list><tree><noCountry><name sortKey="Carver, John A" sort="Carver, John A" uniqKey="Carver J" first="John A" last="Carver">John A. Carver</name><name sortKey="Ecroyd, Heath" sort="Ecroyd, Heath" uniqKey="Ecroyd H" first="Heath" last="Ecroyd">Heath Ecroyd</name><name sortKey="Van Sluyter, Steven" sort="Van Sluyter, Steven" uniqKey="Van Sluyter S" first="Steven" last="Van Sluyter">Steven Van Sluyter</name><name sortKey="Von Smekal, Lorenz" sort="Von Smekal, Lorenz" uniqKey="Von Smekal L" first="Lorenz" last="Von Smekal">Lorenz Von Smekal</name><name sortKey="Waters, Elizabeth J" sort="Waters, Elizabeth J" uniqKey="Waters E" first="Elizabeth J" last="Waters">Elizabeth J. Waters</name></noCountry><country name="Australie"><noRegion><name sortKey="Stranks, Samuel D" sort="Stranks, Samuel D" uniqKey="Stranks S" first="Samuel D" last="Stranks">Samuel D. Stranks</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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