ArticleThe journal of physical chemistry. B2011
Quantitative characterization of temperature-independent and temperature-dependent protein-protein interactions in highly nonideal solutions.
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 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
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- Quantitative characterization of non-specific interaction of two globular proteins with Dextran T70 in a binary mixture.European biophysics journal : EBJ · 2024Article
- Macromolecular Crowding, Phase Separation, and Homeostasis in the Orchestration of Bacterial Cellular Functions.Chemical reviews · 2024Review
- Insights into Protein Stability in Cell Lysate byChembiochem : a European journal of chemical biology · 2020Article
- Particle Detection and Characterization for Biopharmaceutical Applications: Current Principles of Established and Alternative Techniques.Pharmaceutics · 2020Review
- Denaturation studies of Clarias gariepinus glutathione transferase in dilute and crowded solutions.European biophysics journal : EBJ · 2019Article
- Quantitative characterization of temperature-independent polymer-polymer interaction and temperature-dependent protein-protein and protein-polymer interactions in concentrated polymer solutions.European biophysics journal : EBJ · 2019Article
- Weak IgG self- and hetero-association characterized by fluorescence analytical ultracentrifugation.Protein science : a publication of the Protein Society · 2018Article
- 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 effects on two homologs of ribosomal protein s16: protein-dependent structural changes and local interactions.Biophysical journal · 2014Article
- Impact of reconstituted cytosol on protein stability.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Protein-protein interactions in a crowded environment.Biophysical reviews · 2013Review
- Quantitative assessment of the relative contributions of steric repulsion and chemical interactions to macromolecular crowding.Biopolymers · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The interaction among each of three dilute "tracer" proteins (bovine serum albumin, superoxide dismutase, and ovomucoid) at a concentration of 2 mg/mL and each of two "crowder" proteins (ovomucoid and BSA) at concentrations up to 100 mg/mL was characterized by analysis of dependence of the equilibrium gradients of both tracer and crowder upon the concentration of crowder. The equilibrium gradients of both crowder proteins were found to be independent of temperature over the range 5-37 °C. The equilibrium gradients of tracer BSA and ovomucoid in the complementary crowder species were likewise found to be independent of temperature over this range, indicating that interaction among these tracers and crowders is predominantly repulsive and essentially entirely entropic in nature. The equilibrium gradient of tracer SOD in BSA was also found to be independent of temperature over this range, but the gradient of tracer SOD in ovomucoid depended significantly upon temperature in a manner indicating a significant enthalpic (attractive) component of the overall interaction between SOD and ovomucoid. The experimental data are analyzed using model-free expansions of the thermodynamic activity coefficients of tracer and crowder in powers of the concentration of crowder and using approximate statistical thermodynamic models based upon highly simplified descriptions of molecular structure and interactions. Detailed analysis of the results indicates a relatively small contribution of nonspecific attraction to the total protein-protein interaction, which is dominated by steric repulsion.
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Registered trials
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