ArticleThe Journal of chemical physics2022
A retrospective on statistical mechanical models for hemoglobin allostery.
Article in The Journal of chemical physics, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 24 citations in OpenAlex.
- Study of hemoglobin by G. S. Adair and his oxygenation equation: background, history, and significance-on the 100th anniversary of Adair's equation.Biophysical reviews · 2025Review
- Machine learning in molecular biophysics: Protein allostery, multi-level free energy simulations, and lipid phase transitions.Biophysics reviews · 2025Review
- A parameterized two-domain thermodynamic model explains diverse mutational effects on protein allostery.eLife · 2024Article
- A parametrized two-domain thermodynamic model explains diverse mutational effects on protein allostery.bioRxiv : the preprint server for biology · 2024Article
- Application of a novel numerical simulation to biochemical reaction systems.Frontiers in cell and developmental biology · 2024Article
- Ab initio quantification of the oxygen-hemoglobin dissociation curve.Biophysical reports · 2023Article
- Mathematical models describing oxygen binding by hemoglobin.Biophysical reviews · 2023Review
- Modulation of Allosteric Control and Evolution of Hemoglobin.Biomolecules · 2023Review
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1 author at 1 institution in 1 country.
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Abstract
Understanding allosteric interactions in proteins has become one of the major research areas in protein science. The original aim of the famous theoretical model of Monod, Wyman, and Changeux (MWC) was to explain the regulation of enzymatic activity in biochemical pathways. However, its first successful quantitative application was to explain cooperative oxygen binding by hemoglobin, often called the "hydrogen molecule of biology." The combination of its original application and the enormous amount of research on hemoglobin has made it the paradigm for studies of allostery, especially for multi-subunit proteins, and for the development of statistical mechanical models to describe how structure determines function. This article is a historical account of the development of statistical mechanical models for hemoglobin to explain both the cooperative binding of oxygen (called homotropic effects by MWC) and how oxygen binding is affected by ligands that bind distant from the heme oxygen binding site (called heterotropic allosteric effects by MWC). This account makes clear the many remaining challenges for describing the relationship of structure to function for hemoglobin in terms of a satisfactory statistical mechanical model.
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