Allosteric cofactor-mediated enzyme cooperativity: a theoretical treatment.
نویسندگان
چکیده
منابع مشابه
Cooperativity of allosteric receptors.
Cooperativity of ligand binding to allosteric receptors can be quantified using the Hill coefficient (nH) to measure the sigmoidal character of the binding curve. However, for measurements of the transition between conformational states, nH values can be misleading due to ambiguity of the reference state. For cooperative ligand binding, the reference state is a hyperbolic curve for a monomer wi...
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Allosteric signaling in proteins requires long-range communication mediated by highly conserved residues, often triggered by ligand binding. In this article, we map the allosteric network in the catalytic subunit of protein kinase A using NMR spectroscopy. We show that positive allosteric cooperativity is generated by nucleotide and substrate binding during the transitions through the major con...
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Interactions between a protein and a ligand are often accompanied by a redistribution of the population of thermally accessible conformations. This dynamic response of the protein's functional energy landscape enables a protein to modulate binding affinities and control binding sensitivity to ligand concentration. In this paper, we investigate the structural origins of binding affinity and allo...
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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 (measur...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1983
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.80.17.5243