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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<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>
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<term>Scattering, Radiation</term>
<term>Solutions</term>
<term>Sulfhydryl Compounds (analysis)</term>
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<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>
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<term>Réactifs réticulants</term>
<term>Solutions</term>
<term>Spectrométrie de masse</term>
<term>Thiols (analyse)</term>
<term>Électrophorèse sur gel de polyacrylamide</term>
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<term>Electrophoresis, Polyacrylamide Gel</term>
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<term>Conformation des protéines</term>
<term>Cristallines</term>
<term>Diffusion de rayonnements</term>
<term>Dimérisation</term>
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<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>
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<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>
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