ArticleAnalytical biochemistry2008
Measurement of the second osmotic virial coefficient for protein solutions exhibiting monomer-dimer equilibrium.
Article in Analytical biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
16 citing papers in PubMed.
- Monomeric Insulin Analog and Stabilizing Excipient Enabled Ultrafast Insulin Formulation.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Quantitative Perspectives of Biomolecular Crystallization Thermodynamics.Advances in biochemical engineering/biotechnology · 2026Review
- In Situ Online Spectroscopy and Light Scattering Techniques.Advances in biochemical engineering/biotechnology · 2026Review
- HisScientific reports · 2023Article
- Probing interactions of therapeutic antibodies with serum via second virial coefficient measurements.Biophysical journal · 2021Article
- Particle Detection and Characterization for Biopharmaceutical Applications: Current Principles of Established and Alternative Techniques.Pharmaceutics · 2020Review
- Measuring the effects of macromolecular crowding on antibody function with biolayer interferometry.mAbs · 2019Article
- Protein-protein interactions controlling interfacial aggregation of rhIL-1ra are not described by simple colloid models.Protein science : a publication of the Protein Society · 2018Article
- Silk-based stabilization of biomacromolecules.Journal of controlled release : official journal of the Controlled Release Society · 2015Review
- The second virial coefficient as a predictor of protein aggregation propensity: A self-interaction chromatography study.European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V · 2015Article
- Effects of ionic strength and sugars on the aggregation propensity of monoclonal antibodies: influence of colloidal and conformational stabilities.Pharmaceutical research · 2013Article
- Behavior of monoclonal antibodies: relation between the second virial coefficient (B (2)) at low concentrations and aggregation propensity and viscosity at high concentrations.Pharmaceutical research · 2012Article
- High-throughput protein purification and quality assessment for crystallization.Methods (San Diego, Calif.) · 2011Review
- Reexamining protein-protein and protein-solvent interactions from Kirkwood-Buff analysis of light scattering in multi-component solutions.The Journal of chemical physics · 2011Article
- Selecting temperature for protein crystallization screens using the temperature dependence of the second virial coefficient.PloS one · 2011Article
- Review
Corrections and comments
- Erratum issued
Authors and funding
4 authors.
Funding
Abstract
The second osmotic virial coefficient (B) is a measure of solution nonideality that is useful for predicting conditions favorable for protein crystallization and for inhibition of aggregation. Static light scattering is the technique most commonly used to determine B values, typically using protein concentrations less than 5 mg/mL. During static light scattering experiments at low protein concentrations, frequently the protein is assumed to exist either as a single nonassociating species or as a combination of assembly states independent of protein concentration. In the work described here, we examined the limit for ignoring weak reversible dimerization (Kd > or =1 mM) by comparing B values calculated with and without accounting for self-association. Light scattering effects for equilibrium dimer systems with Kd <20 mM and Kd <1 mM will significantly affect apparent B values measured for 20 and 150-kDa proteins, respectively. To interpret correctly light scattering data for monomer-dimer equilibrium systems, we use an expanded coefficient model to account for separate monomer-monomer (B(22)), monomer-dimer (B(23)), and dimer-dimer (B(33)) interactions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.