A model of cooperativity based on restricted binding: kinetic and thermodynamic analysis

DOI10.1007/S10910-013-0292-YMaRDI QIDQ2014797zbMATH OpenOpenAlexFDO

Authors Kinshuk Banerjee

Publication date 16 June 2014

Published in Journal of Mathematical Chemistry (Search for Journal in Brave)

Full work available at URL https://doi.org/10.1007/s10910-013-0292-y

zbMATH Keywords

master equationcooperativityoligomeric proteinstochastic thermodynamics

Mathematics Subject Classification ID

Molecular structure (graph-theoretic methods, methods of differential topology, etc.) (92E10) Classical flows, reactions, etc. in chemistry (92E20)

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Cites work

• scientific article; zbMATH DE number 1161490 (Why is no real title available?)
• A Gallavotti-Cohen-type symmetry in the large deviation functional for stochastic dynamics
• Entropy production for mechanically or chemically driven biomolecules
• Extension of Onsager's Reciprocity to Large Fields and the Chaotic Hypothesis
• Probability of second law violations in shearing steady states

Cited in

(9)

• Analysing protein energy data by a stochastic model for cooperative interactions: comparison and characterization of cooperativity
• A measure to quantify the degree of cooperativity in overall titration curves
• On the relation of different definitions of cooperative binding for systems with two binding sites
• An asymptotic comparative analysis of the thermodynamics of non-covalent association
• On Hill coefficients and subunit interaction energies
• A model for cooperative ligand binding at complementary sites of DNA
• A MARKOVIAN MODEL FOR COOPERATIVE INTERACTIONS IN PROTEINS
• Minimal models of multi-site ligand-binding kinetics
• The significance of noise in the evolution of negative and positive cooperativity in protein complexes

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