Oligomerization and phase separation in globular protein solutions.
Identifieur interne : 002651 ( PubMed/Corpus ); précédent : 002650; suivant : 002652Oligomerization and phase separation in globular protein solutions.
Auteurs : N. Asherie ; J. Pande ; A. Lomakin ; O. Ogun ; S R Hanson ; J B Smith ; G B BenedekSource :
- Biophysical chemistry [ 0301-4622 ] ; 1998.
English descriptors
- KwdEn :
- Animals, Cattle, Chemical Phenomena, Chemistry, Physical, Chromatography, High Pressure Liquid, Cross-Linking Reagents, Crystallins (chemistry), Crystallins (isolation & purification), Dimerization, Electrophoresis, Polyacrylamide Gel, Light, Maleimides, Mass Spectrometry, Molecular Weight, Protein Conformation, Scattering, Radiation, Solutions, Sulfhydryl Compounds (analysis).
- MESH :
- chemical , analysis : Sulfhydryl Compounds.
- chemical , chemistry : Crystallins.
- chemical , isolation & purification : Crystallins.
- chemical : Cross-Linking Reagents, Maleimides, Solutions.
- Animals, Cattle, Chemical Phenomena, Chemistry, Physical, Chromatography, High Pressure Liquid, Dimerization, Electrophoresis, Polyacrylamide Gel, Light, Mass Spectrometry, Molecular Weight, Protein Conformation, Scattering, Radiation.
Abstract
We have chemically crosslinked a globular protein, gamma IIIb-crystallin, to produce a system of well-defined oligomers: monomers, dimers, trimers and a mixture of higher n-mers. Gel electrophoresis, size exclusion chromatography, quasielastic light scattering spectroscopy, and electrospray ionization mass spectrometry were used to characterize the oligomers formed. The liquid-liquid phase separation boundaries of the various oligomers were measured. We find that at a given concentration the phase separation temperature strongly increases with the molecular weight of the oligomers. This phase behavior is very similar to previous findings for gamma II-crystallin, for which oxidation-induced oligomerization is accompanied by an increase in the phase separation temperature. These findings imply that for phase separation, the detailed changes of the surface properties of the proteins are less important than the purely steric effects of oligomerization.
DOI: 10.1016/s0301-4622(98)00208-7
PubMed: 9894340
Links to Exploration step
pubmed:9894340Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Oligomerization and phase separation in globular protein solutions.</title>
<author><name sortKey="Asherie, N" sort="Asherie, N" uniqKey="Asherie N" first="N" last="Asherie">N. Asherie</name>
<affiliation><nlm:affiliation>Department of Physics, Massachusetts Institute of Technology, Cambridge 02139-4307, USA.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Pande, J" sort="Pande, J" uniqKey="Pande J" first="J" last="Pande">J. Pande</name>
</author>
<author><name sortKey="Lomakin, A" sort="Lomakin, A" uniqKey="Lomakin A" first="A" last="Lomakin">A. Lomakin</name>
</author>
<author><name sortKey="Ogun, O" sort="Ogun, O" uniqKey="Ogun O" first="O" last="Ogun">O. Ogun</name>
</author>
<author><name sortKey="Hanson, S R" sort="Hanson, S R" uniqKey="Hanson S" first="S R" last="Hanson">S R Hanson</name>
</author>
<author><name sortKey="Smith, J B" sort="Smith, J B" uniqKey="Smith J" first="J B" last="Smith">J B Smith</name>
</author>
<author><name sortKey="Benedek, G B" sort="Benedek, G B" uniqKey="Benedek G" first="G B" last="Benedek">G B Benedek</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="1998">1998</date>
<idno type="RBID">pubmed:9894340</idno>
<idno type="pmid">9894340</idno>
<idno type="doi">10.1016/s0301-4622(98)00208-7</idno>
<idno type="wicri:Area/PubMed/Corpus">002651</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002651</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Oligomerization and phase separation in globular protein solutions.</title>
<author><name sortKey="Asherie, N" sort="Asherie, N" uniqKey="Asherie N" first="N" last="Asherie">N. Asherie</name>
<affiliation><nlm:affiliation>Department of Physics, Massachusetts Institute of Technology, Cambridge 02139-4307, USA.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Pande, J" sort="Pande, J" uniqKey="Pande J" first="J" last="Pande">J. Pande</name>
</author>
<author><name sortKey="Lomakin, A" sort="Lomakin, A" uniqKey="Lomakin A" first="A" last="Lomakin">A. Lomakin</name>
</author>
<author><name sortKey="Ogun, O" sort="Ogun, O" uniqKey="Ogun O" first="O" last="Ogun">O. Ogun</name>
</author>
<author><name sortKey="Hanson, S R" sort="Hanson, S R" uniqKey="Hanson S" first="S R" last="Hanson">S R Hanson</name>
</author>
<author><name sortKey="Smith, J B" sort="Smith, J B" uniqKey="Smith J" first="J B" last="Smith">J B Smith</name>
</author>
<author><name sortKey="Benedek, G B" sort="Benedek, G B" uniqKey="Benedek G" first="G B" last="Benedek">G B Benedek</name>
</author>
</analytic>
<series><title level="j">Biophysical chemistry</title>
<idno type="ISSN">0301-4622</idno>
<imprint><date when="1998" type="published">1998</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Cattle</term>
<term>Chemical Phenomena</term>
<term>Chemistry, Physical</term>
<term>Chromatography, High Pressure Liquid</term>
<term>Cross-Linking Reagents</term>
<term>Crystallins (chemistry)</term>
<term>Crystallins (isolation & purification)</term>
<term>Dimerization</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Light</term>
<term>Maleimides</term>
<term>Mass Spectrometry</term>
<term>Molecular Weight</term>
<term>Protein Conformation</term>
<term>Scattering, Radiation</term>
<term>Solutions</term>
<term>Sulfhydryl Compounds (analysis)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Sulfhydryl Compounds</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Crystallins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Crystallins</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Cross-Linking Reagents</term>
<term>Maleimides</term>
<term>Solutions</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cattle</term>
<term>Chemical Phenomena</term>
<term>Chemistry, Physical</term>
<term>Chromatography, High Pressure Liquid</term>
<term>Dimerization</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Light</term>
<term>Mass Spectrometry</term>
<term>Molecular Weight</term>
<term>Protein Conformation</term>
<term>Scattering, Radiation</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">We have chemically crosslinked a globular protein, gamma IIIb-crystallin, to produce a system of well-defined oligomers: monomers, dimers, trimers and a mixture of higher n-mers. Gel electrophoresis, size exclusion chromatography, quasielastic light scattering spectroscopy, and electrospray ionization mass spectrometry were used to characterize the oligomers formed. The liquid-liquid phase separation boundaries of the various oligomers were measured. We find that at a given concentration the phase separation temperature strongly increases with the molecular weight of the oligomers. This phase behavior is very similar to previous findings for gamma II-crystallin, for which oxidation-induced oligomerization is accompanied by an increase in the phase separation temperature. These findings imply that for phase separation, the detailed changes of the surface properties of the proteins are less important than the purely steric effects of oligomerization.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9894340</PMID>
<DateCompleted><Year>1999</Year>
<Month>02</Month>
<Day>19</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>08</Month>
<Day>31</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">0301-4622</ISSN>
<JournalIssue CitedMedium="Print"><Volume>75</Volume>
<Issue>3</Issue>
<PubDate><Year>1998</Year>
<Month>Dec</Month>
<Day>14</Day>
</PubDate>
</JournalIssue>
<Title>Biophysical chemistry</Title>
<ISOAbbreviation>Biophys. Chem.</ISOAbbreviation>
</Journal>
<ArticleTitle>Oligomerization and phase separation in globular protein solutions.</ArticleTitle>
<Pagination><MedlinePgn>213-27</MedlinePgn>
</Pagination>
<Abstract><AbstractText>We have chemically crosslinked a globular protein, gamma IIIb-crystallin, to produce a system of well-defined oligomers: monomers, dimers, trimers and a mixture of higher n-mers. Gel electrophoresis, size exclusion chromatography, quasielastic light scattering spectroscopy, and electrospray ionization mass spectrometry were used to characterize the oligomers formed. The liquid-liquid phase separation boundaries of the various oligomers were measured. We find that at a given concentration the phase separation temperature strongly increases with the molecular weight of the oligomers. This phase behavior is very similar to previous findings for gamma II-crystallin, for which oxidation-induced oligomerization is accompanied by an increase in the phase separation temperature. These findings imply that for phase separation, the detailed changes of the surface properties of the proteins are less important than the purely steric effects of oligomerization.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Asherie</LastName>
<ForeName>N</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Department of Physics, Massachusetts Institute of Technology, Cambridge 02139-4307, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Pande</LastName>
<ForeName>J</ForeName>
<Initials>J</Initials>
</Author>
<Author ValidYN="Y"><LastName>Lomakin</LastName>
<ForeName>A</ForeName>
<Initials>A</Initials>
</Author>
<Author ValidYN="Y"><LastName>Ogun</LastName>
<ForeName>O</ForeName>
<Initials>O</Initials>
</Author>
<Author ValidYN="Y"><LastName>Hanson</LastName>
<ForeName>S R</ForeName>
<Initials>SR</Initials>
</Author>
<Author ValidYN="Y"><LastName>Smith</LastName>
<ForeName>J B</ForeName>
<Initials>JB</Initials>
</Author>
<Author ValidYN="Y"><LastName>Benedek</LastName>
<ForeName>G B</ForeName>
<Initials>GB</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>EY05127</GrantID>
<Acronym>EY</Acronym>
<Agency>NEI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>EY07609</GrantID>
<Acronym>EY</Acronym>
<Agency>NEI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>EY10535</GrantID>
<Acronym>EY</Acronym>
<Agency>NEI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType>
</PublicationTypeList>
</Article>
<MedlineJournalInfo><Country>Netherlands</Country>
<MedlineTA>Biophys Chem</MedlineTA>
<NlmUniqueID>0403171</NlmUniqueID>
<ISSNLinking>0301-4622</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D003432">Cross-Linking Reagents</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D003459">Crystallins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D008301">Maleimides</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D012996">Solutions</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D013438">Sulfhydryl Compounds</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>4856-87-5</RegistryNumber>
<NameOfSubstance UI="C075594">1,6-bismaleimidohexane</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002417" MajorTopicYN="N">Cattle</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D055598" MajorTopicYN="N">Chemical Phenomena</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002627" MajorTopicYN="N">Chemistry, Physical</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003432" MajorTopicYN="N">Cross-Linking Reagents</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003459" MajorTopicYN="N">Crystallins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008027" MajorTopicYN="N">Light</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008301" MajorTopicYN="N">Maleimides</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012542" MajorTopicYN="N">Scattering, Radiation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012996" MajorTopicYN="N">Solutions</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName>
<QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1999</Year>
<Month>1</Month>
<Day>23</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>1999</Year>
<Month>1</Month>
<Day>23</Day>
<Hour>0</Hour>
<Minute>1</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>1999</Year>
<Month>1</Month>
<Day>23</Day>
<Hour>0</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">9894340</ArticleId>
<ArticleId IdType="pii">S0301462298002087</ArticleId>
<ArticleId IdType="doi">10.1016/s0301-4622(98)00208-7</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/PubMed/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002651 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 002651 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= MersV1 |flux= PubMed |étape= Corpus |type= RBID |clé= pubmed:9894340 |texte= Oligomerization and phase separation in globular protein solutions. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:9894340" \ | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \ | NlmPubMed2Wicri -a MersV1
This area was generated with Dilib version V0.6.33. |