ArticleThe journal of physical chemistry. B2009
pH-dependent association of proteins. The test case of monoclonal antibody HyHEL-5 and its antigen hen egg white lysozyme.
Article in The journal of physical chemistry. B, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed, 5 citations in OpenAlex.
- Article
- Effect of medium pH and antibody Fc fragment on the size of model immune complexes.Doklady. Biochemistry and biophysics · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We describe a method for determining diffusion-controlled rate constants for protein-protein association that explicitly includes the solution pH. The method combines the transient-complex theory for computing electrostatically enhanced association rates with an approach based on a rigorous thermodynamic cycle and partition functions for energy levels characterizing protonation states of associating proteins and their complexes. To test our method, we determine the pH-dependent kinetics of association of the HyHEL-5 antibody with its antigen hen egg white lysozyme. It was shown experimentally that their association rate constant depends on pH, increasing linearly in the pH range 6-8 and saturating or even exhibiting a flat maximum in the pH range 8-10. The presented methodology leads to a qualitative agreement with the experimental data. Our approach allows one to study diffusion-controlled protein-protein association under different pH conditions by taking into account the ensembles of protonation states rather than just the most probable protonation state of each protein.
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