ArticleThe journal of physical chemistry. B2011
Effect of nonadditive repulsive intermolecular interactions on the light scattering of concentrated protein-osmolyte mixtures.
Article in The journal of physical chemistry. B, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- 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
- TMAO-Protein Preferential Interaction Profile Determines TMAO's Conditional In Vivo Compatibility.Biophysical journal · 2016Article
- 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
- Quantitative characterization of the compensating effects of trimethylamine-N-oxide and guanidine hydrochloride on the dissociation of human cyanmethmoglobin.The journal of physical chemistry. B · 2013Article
- Compensating effects of urea and trimethylamine-N-oxide on the heteroassociation of α-chymotrypsin and soybean trypsin inhibitor.The journal of physical chemistry. B · 2013Article
- Quantitative assessment of the relative contributions of steric repulsion and chemical interactions to macromolecular crowding.Biopolymers · 2013Article
- Influences of excluded volume of molecules on signaling processes on the biomembrane.PloS one · 2013Article
- Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The static light scattering of three globular proteins, bovine serum albumin, ovalbumin, and ovomucoid, and binary mixtures of each protein and trimethylamine oxide (TMAO) containing between 10 and 70% protein, were measured as a function of total weight per volume concentration up to 100 g/L. The observed dependence of scattering upon concentration may be accounted for quantitatively by an effective hard sphere model incorporating an extension that takes into account the nonadditive nature of the repulsive intermolecular interaction between protein and TMAO.
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Registered trials
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