ArticleProtein science : a publication of the Protein Society2022
Partitioning the Hill coefficient into contributions from ligand-promoted conformational changes and subunit heterogeneity.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 10 citations in OpenAlex.
- On the relationship between efficiency and cooperativity in multi-subunit molecular machines.Protein science : a publication of the Protein Society · 2026Article
- Feedback Control and Sensitivity Analysis in Synthetic Gene Circuits.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Merging different allosteric mechanisms: The case ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Roles of Hydration in Protein-Ligand Binding: Passive or Active Participant?The journal of physical chemistry. A · 2025Article
- Predicting residue ionization of OmpF channel using Constant pH Molecular Dynamics as benchmark.PLoS computational biology · 2025Article
- Allostery without Conformational Change: A Native Mass Spectrometry Perspective.The journal of physical chemistry. B · 2025Article
- On the Rational Design of Cooperative Receptors.Annual review of biophysics · 2023Review
- Analysis of continuous enzyme kinetic data using ICEKAT.Methods in enzymology · 2023Article
- Partitioning the Hill coefficient into contributions from ligand-promoted conformational changes and subunit heterogeneity.Protein science : a publication of the Protein Society · 2022Article
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2 authors at 1 institution in 1 country.
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Abstract
Heterooligomers that undergo ligand-promoted conformational changes are ubiquitous in nature and involved in many essential processes. Conformational switching often leads to positive cooperativity in ligand binding that is reflected in a Hill coefficient with a value greater than one. The subunits comprising heterooligomers can differ, however, in their affinity for the ligand. Such so-called site heterogeneity results in apparent negative cooperativity that is reflected by a Hill coefficient with a value less than one. Consequently, positive cooperativity due to the ligand-promoted allosteric switch can be masked, in cases of such heterooligomers, by apparent negative cooperativity owing to site heterogeneity. Here, we derived expressions for the Hill coefficient, in the case of a heterodimer, in which the contributions from the ligand-promoted allosteric switch and site heterogeneity are separated. Using these equations and simulations for higher order oligomers, we show under which conditions site heterogeneity can significantly mask the extent of observed positive cooperativity.
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