Oligomerization and phase separation in globular protein solutions
| Autor: | Stacy R.A. Hanson, Neer Asherie, Olutayo Ogun, George B. Benedek, Jayanti Pande, Jean B. Smith, Aleksey Lomakin |
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| Rok vydání: | 1998 |
| Předmět: |
Steric effects
Chemical Phenomena Light Protein Conformation Globular protein Electrospray ionization Size-exclusion chromatography Biophysics Analytical chemistry Mass spectrometry Biochemistry Mass Spectrometry Maleimides chemistry.chemical_compound Protein structure Phase (matter) Animals Scattering Radiation Sulfhydryl Compounds Chromatography High Pressure Liquid chemistry.chemical_classification Chemistry Physical Organic Chemistry Crystallins Molecular Weight Solutions Crystallography Cross-Linking Reagents Monomer chemistry Cattle Electrophoresis Polyacrylamide Gel Dimerization |
| Zdroj: | Biophysical Chemistry. 75:213-227 |
| ISSN: | 0301-4622 |
| DOI: | 10.1016/s0301-4622(98)00208-7 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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