ArticleThe Journal of chemical physics2011
Reexamining protein-protein and protein-solvent interactions from Kirkwood-Buff analysis of light scattering in multi-component solutions.
Article in The Journal of chemical physics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- A historical overview of the need for distinction between the attainment of thermodynamic equilibrium and a kinetic steady state in experimental studies.European biophysics journal : EBJ · 2026Review
- Structural Properties of [N1888][TFSI] Ionic Liquid: A Small Angle Neutron Scattering and Polarizable Molecular Dynamics Study.The journal of physical chemistry. B · 2024Article
- The molecular basis for hydrodynamic properties of PEGylated human serum albumin.Biophysical journal · 2024Article
- The origins of nonideality exhibited by monoclonal antibodies and Fab fragments in human serum.Protein science : a publication of the Protein Society · 2023Article
- Role of Domain-Domain Interactions on the Self-Association and Physical Stability of Monoclonal Antibodies: Effect of pH and Salt.The journal of physical chemistry. B · 2023Article
- The Relationship between Protein-Protein Interactions and Liquid-Liquid Phase Separation for Monoclonal Antibodies.Molecular pharmaceutics · 2023Article
- Anomalous Concentration Dependence of Surface Tension and Concentration-Concentration Correlation Functions of Binary Non-Electrolyte Solutions.International journal of molecular sciences · 2023Article
- Use of Debye-Hückel-Henry charge measurements in early antibody development elucidates effects of non-specific association.Antibody therapeutics · 2022Article
- Quantifying Protein-Protein Interactions in Molecular Simulations.The journal of physical chemistry. B · 2020Article
- Experimental determination of second virial coefficients by small-angle X-ray scattering: a problem revisited.European biophysics journal : EBJ · 2019Article
- Evaluating the Effects of Hinge Flexibility on the Solution Structure of Antibodies at Concentrated Conditions.Journal of pharmaceutical sciences · 2019Article
- A Reappraisal of Sedimentation Nonideality Coefficients for the Analysis of Weak Interactions of Therapeutic Proteins.The AAPS journal · 2019Article
- Measuring macromolecular size distributions and interactions at high concentrations by sedimentation velocity.Nature communications · 2018Article
- Biophysical characterization and molecular simulation of electrostatically driven self-association of a single-chain antibody.Protein science : a publication of the Protein Society · 2018Article
- Predicting Protein-Protein Interactions of Concentrated Antibody Solutions Using Dilute Solution Data and Coarse-Grained Molecular Models.Journal of pharmaceutical sciences · 2018Article
- Effect of the surface charge distribution on the fluid phase behavior of charged colloids and proteins.The Journal of chemical physics · 2016Article
- Modulating non-native aggregation and electrostatic protein-protein interactions with computationally designed single-point mutations.Protein engineering, design & selection : PEDS · 2016Article
- Recent applications of light scattering measurement in the biological and biopharmaceutical sciences.Analytical biochemistry · 2016Review
- Article
- Determination of the second virial coefficient of bovine serum albumin under varying pH and ionic strength by composition-gradient multi-angle static light scattering.Journal of biological physics · 2015Article
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4 authors.
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Abstract
The classic analysis of Rayleigh light scattering (LS) is re-examined for multi-component protein solutions, within the context of Kirkwood-Buff (KB) theory as well as a more generalized canonical treatment. Significant differences arise when traditional treatments that approximate constant pressure and neglect concentration fluctuations in one or more (co)solvent/co-solute species are compared with more rigorous treatments at constant volume and with all species free to fluctuate. For dilute solutions, it is shown that LS can be used to rigorously and unambiguously obtain values for the osmotic second virial coefficient (B(22)), in contrast with recent arguments regarding protein interactions deduced from LS experiments. For more concentrated solutions, it is shown that conventional analysis over(under)-estimates the magnitude of B(22) for significantly repulsive(attractive) conditions, and that protein-protein KB integrals (G(22)) are the more relevant quantity obtainable from LS. Published data for α-chymotrypsinogen A and a series of monoclonal antibodies at different pH and salt concentrations are re-analyzed using traditional and new treatments. The results illustrate that while traditional analysis may be sufficient if one is interested in only the sign of B(22) or G(22), the quantitative values can be significantly in error. A simple approach is illustrated for determining whether protein concentration (c(2)) is sufficiently dilute for B(22) to apply, and for correcting B(22) values from traditional LS regression at higher c(2) values. The apparent molecular weight M(2, app) obtained from LS is shown to generally not be equal to the true molecular weight, with the differences arising from a combination of protein-solute and protein-cosolute interactions that may, in principle, also be determined from LS.
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