ArticleBiophysical journal2009
Static light scattering from concentrated protein solutions II: experimental test of theory for protein mixtures and weakly self-associating proteins.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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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
25 citing papers in PubMed, 67 citations in OpenAlex.
- Review
- Effects of Cascading Optical Processes: Part I: Impacts on Quantification of Sample Scattering Extinction, Intensity, and Depolarization.Analytical chemistry · 2023Article
- Global multi-method analysis of interaction parameters for reversibly self-associating macromolecules at high concentrations.Scientific reports · 2021Article
- Article
- The Cumulative Effect of Surface Adsorption and Excluded Volume in 2D and 3D on Protein Fibrillation.Biophysical journal · 2019Article
- Non-specific Interactions Between Macromolecular Solutes in Concentrated Solution: Physico-Chemical Manifestations and Biochemical Consequences.Frontiers in molecular biosciences · 2019Article
- Toward an understanding of biochemical equilibria within living cells.Biophysical reviews · 2018Review
- Explicit Incorporation of Hard and Soft Protein-Protein Interactions into Models for Crowding Effects in Protein Mixtures. 2. Effects of Varying Hard and Soft Interactions upon Prototypical Chemical Equilibria.The journal of physical chemistry. B · 2017Article
- Macromolecular Crowding In Vitro, In Vivo, and In Between.Trends in biochemical sciences · 2016Review
- Charged Molecules Modulate the Volume Exclusion Effects Exerted by Crowders on FtsZ Polymerization.PloS one · 2016Article
- 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
- Combined dynamic light scattering and Raman spectroscopy approach for characterizing the aggregation of therapeutic proteins.Molecules (Basel, Switzerland) · 2014Article
- Protein aggregation and its impact on product quality.Current opinion in biotechnology · 2014Review
- Role of anisotropic interactions for proteins and patchy nanoparticles.The journal of physical chemistry. B · 2014Article
- Light-scattering-based analysis of biomolecular interactions.Biophysical reviews · 2013Article
- Quantitative assessment of the relative contributions of steric repulsion and chemical interactions to macromolecular crowding.Biopolymers · 2013Article
- Quantitative characterization of temperature-independent and temperature-dependent protein-protein interactions in highly nonideal solutions.The journal of physical chemistry. B · 2011Article
- Effect of sugar molecules on the viscosity of high concentration monoclonal antibody solutions.Pharmaceutical research · 2011Article
- Reexamining protein-protein and protein-solvent interactions from Kirkwood-Buff analysis of light scattering in multi-component solutions.The Journal of chemical physics · 2011Article
- On the distribution of protein refractive index increments.Biophysical journal · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Using an experimental technique recently developed in this laboratory (Fernández C. and A. P. Minton. 2008. Anal. Biochem. 381:254-257), the Rayleigh light scattering of solutions of bovine serum albumin, hen egg white ovalbumin, hen egg white ovomucoid, and binary mixtures of these three proteins was measured as a function of concentration at concentrations up to 125 g/L. The measured concentration dependence of scattering of both pure proteins and binary mixtures is accounted for nearly quantitatively by an effective hard particle model (Minton A. P. 2007. Biophys. J. 93:1321-1328) in which each protein species is represented by an equivalent hard sphere, the size of which is determined by the nature of repulsive interactions between like molecules under a given set of experimental conditions. The light scattering of solutions of chymotrypsin A was measured as a function of concentration at concentrations up to 70 g/L at pH 4.1, 5.4, and 7.2. At each pH, the measured concentration dependence is accounted for quantitatively by an effective hard particle model, according to which monomeric protein may self-associate to form an equilibrium dimer and, depending upon pH, an equilibrium pentamer or hexamer.
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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.