ArticleJournal of molecular biology2014
A novel equation for cooperativity of the allosteric state function.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Mathematical models describing oxygen binding by hemoglobin.Biophysical reviews · 2023Review
- Biased Allostery.Biophysical journal · 2016Article
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1 author.
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Abstract
The MWC (Monod-Wyman-Changeux) allosteric model postulates concerted conformational changes between two states: the intrinsically more stable T state with relatively weak ligand binding and the R state with relatively strong ligand binding. The model distinguishes between Y¯ (the fractional occupation of the binding sites) and R¯ (the fraction of molecules in the R state). Cooperativity (measured by the Hill coefficient) has strikingly different properties for Y¯ and R¯. For the latter, cooperativity depends only on the relative affinities of the two states, not on their relative intrinsic stabilities, as demonstrated here with a simple new equation relating the Hill coefficient to R¯.
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