Oligomerization and phase separation in globular protein solutions.
Identifieur interne : 003990 ( Main/Exploration ); précédent : 003989; suivant : 003991Oligomerization and phase separation in globular protein solutions.
Auteurs : N. Asherie [États-Unis] ; J. Pande ; A. Lomakin ; O. Ogun ; S R Hanson ; J B Smith ; G B BenedekSource :
- Biophysical chemistry [ 0301-4622 ] ; 1998.
Descripteurs français
- KwdFr :
- Animaux, Bovins, Chimie physique, Chromatographie en phase liquide à haute performance, Conformation des protéines, Cristallines (), Cristallines (isolement et purification), Diffusion de rayonnements, Dimérisation, Lumière, Maléimides, Masse moléculaire, Phénomènes chimiques, Réactifs réticulants, Solutions, Spectrométrie de masse, Thiols (analyse), Électrophorèse sur gel de polyacrylamide.
- MESH :
- analyse : Thiols.
- isolement et purification : Cristallines.
- Animaux, Bovins, Chimie physique, Chromatographie en phase liquide à haute performance, Conformation des protéines, Cristallines, Diffusion de rayonnements, Dimérisation, Lumière, Maléimides, Masse moléculaire, Phénomènes chimiques, Réactifs réticulants, Solutions, Spectrométrie de masse, Électrophorèse sur gel de polyacrylamide.
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
Affiliations:
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Le document en format XML
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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><idno type="wicri:Area/PubMed/Curation">002651</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002651</idno><idno type="wicri:Area/PubMed/Checkpoint">002520</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002520</idno><idno type="wicri:Area/Ncbi/Merge">002B53</idno><idno type="wicri:Area/Ncbi/Curation">002B53</idno><idno type="wicri:Area/Ncbi/Checkpoint">002B53</idno><idno type="wicri:doubleKey">0301-4622:1998:Asherie N:oligomerization:and:phase</idno><idno type="wicri:Area/Main/Merge">003A37</idno><idno type="wicri:Area/Main/Curation">003990</idno><idno type="wicri:Area/Main/Exploration">003990</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 wicri:level="1"><nlm:affiliation>Department of Physics, Massachusetts Institute of Technology, Cambridge 02139-4307, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Physics, Massachusetts Institute of Technology, Cambridge 02139-4307</wicri:regionArea><wicri:noRegion>Cambridge 02139-4307</wicri:noRegion></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="KwdFr" xml:lang="fr"><term>Animaux</term><term>Bovins</term><term>Chimie physique</term><term>Chromatographie en phase liquide à haute performance</term><term>Conformation des protéines</term><term>Cristallines ()</term><term>Cristallines (isolement et purification)</term><term>Diffusion de rayonnements</term><term>Dimérisation</term><term>Lumière</term><term>Maléimides</term><term>Masse moléculaire</term><term>Phénomènes chimiques</term><term>Réactifs réticulants</term><term>Solutions</term><term>Spectrométrie de masse</term><term>Thiols (analyse)</term><term>Électrophorèse sur gel de polyacrylamide</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" qualifier="analyse" xml:lang="fr"><term>Thiols</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Cristallines</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><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Bovins</term><term>Chimie physique</term><term>Chromatographie en phase liquide à haute performance</term><term>Conformation des protéines</term><term>Cristallines</term><term>Diffusion de rayonnements</term><term>Dimérisation</term><term>Lumière</term><term>Maléimides</term><term>Masse moléculaire</term><term>Phénomènes chimiques</term><term>Réactifs réticulants</term><term>Solutions</term><term>Spectrométrie de masse</term><term>Électrophorèse sur gel de polyacrylamide</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><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Benedek, G B" sort="Benedek, G B" uniqKey="Benedek G" first="G B" last="Benedek">G B Benedek</name><name sortKey="Hanson, S R" sort="Hanson, S R" uniqKey="Hanson S" first="S R" last="Hanson">S R Hanson</name><name sortKey="Lomakin, A" sort="Lomakin, A" uniqKey="Lomakin A" first="A" last="Lomakin">A. Lomakin</name><name sortKey="Ogun, O" sort="Ogun, O" uniqKey="Ogun O" first="O" last="Ogun">O. Ogun</name><name sortKey="Pande, J" sort="Pande, J" uniqKey="Pande J" first="J" last="Pande">J. Pande</name><name sortKey="Smith, J B" sort="Smith, J B" uniqKey="Smith J" first="J B" last="Smith">J B Smith</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Asherie, N" sort="Asherie, N" uniqKey="Asherie N" first="N" last="Asherie">N. Asherie</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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