ArticleProceedings of the National Academy of Sciences of the United States of America2014
Experimental basis for a new allosteric model for multisubunit proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- Two birds with one stone: An antibiotic hit blockingiScience · 2026Article
- Framework for Quantifying the Efficiency of Competing Signal Transmission Modes in Proteins.Journal of the American Chemical Society · 2026Article
- Hemoglobin receptor redundancy inJournal of structural biology: X · 2025Article
- Direct observation of two-channel photodissociation of carbon monoxide from the hemoglobin subunits.Nature communications · 2025Article
- Analysis of β-C-terminal salt bridges in T-state hemoglobin by trapping tertiary conformations in silica gels.Protein science : a publication of the Protein Society · 2025Article
- Effects of allosteric effectors on oxygen binding to crystals of hemoglobin in the R-quaternary structure.Protein science : a publication of the Protein Society · 2025Article
- Modeling the mechanism of Ca2+ release in skeletal muscle by DHPRs easing inhibition at RyR I1-sites.The Journal of general physiology · 2024Article
- Is allostery a fuzzy concept?FEBS open bio · 2024Review
- A parameterized two-domain thermodynamic model explains diverse mutational effects on protein allostery.eLife · 2024Article
- Identification of small molecules affecting the interaction between human hemoglobin and Staphylococcus aureus IsdB hemophore.Scientific reports · 2024Article
- A parametrized two-domain thermodynamic model explains diverse mutational effects on protein allostery.bioRxiv : the preprint server for biology · 2024Article
- A retrospective on statistical mechanical models for hemoglobin allostery.The Journal of chemical physics · 2022Article
- Impact of hemoglobin biophysical studies on molecular pathogenesis and drug therapy for sickle cell disease.Molecular aspects of medicine · 2022Review
- Structural origin of cooperativity in human hemoglobin: a view from different roles of α and β subunits in the αBiophysical reviews · 2022Review
- Article
- Drug discovery by a basic research scientist.Frontiers in molecular biosciences · 2022Article
- Towards understanding non-equivalence of α and β subunits within human hemoglobin in conformational relaxation and molecular oxygen rebinding.Chemical science · 2021Article
- Article
- Haemoglobin(βK120C)-albumin trimer as an artificial ORSC chemical biology · 2020Article
- Allosteric control of hemoglobin S fiber formation by oxygen and its relation to the pathophysiology of sickle cell disease.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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7 authors.
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Abstract
Monod, Wyman, and Changeux (MWC) explained allostery in multisubunit proteins with a widely applied theoretical model in which binding of small molecules, so-called allosteric effectors, affects reactivity by altering the equilibrium between more reactive (R) and less reactive (T) quaternary structures. In their model, each quaternary structure has a single reactivity. Here, we use silica gels to trap protein conformations and a new kind of laser photolysis experiment to show that hemoglobin, the paradigm of allostery, exhibits two ligand binding phases with the same fast and slow rates in both R and T quaternary structures. Allosteric effectors change the fraction of each phase but not the rates. These surprising results are readily explained by the simplest possible extension of the MWC model to include a preequilibrium between two tertiary conformations that have the same functional properties within each quaternary structure. They also have important implications for the long-standing question of a structural explanation for the difference in hemoglobin oxygen affinity of the two quaternary structures.
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