Kinetic models: Enzyme Catalysis and Mass Action Laws

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Page 3 of 4

Explores the history of catalysis, Nobel Prizes in the field, types of catalysis, and modern challenges.

Explores enzymatic catalysis mechanisms and inhibition dynamics in catalysis and polymerization.

Introduces the fundamental concepts of metabolism, including metabolic pathways, bioenergetics, ATP role, and enzyme catalysis.

Delves into enzyme kinetics, emphasizing how enzymes influence reaction rates through substrate concentration and the Michaelis-Menten equation.

Explores the kinetics of covalent inhibitors, focusing on compounds A and B.

Examines stochastic chemical reactions, from spatial models to enzyme kinetics, including the impact of crowding on reactions.

Explores reaction kinetics, rate laws, reversible reactions, and complex mechanisms, including parallel and consecutive reactions.

Explores chemical kinetics, covering reaction rates, mechanisms, and factors influencing reaction speeds.

Explores reversible reactions, equilibrium, energy barriers, and reaction rates based on concentration and temperature effects.

Explores Michaelis-Menten enzymatic kinetics, steady-state, enzyme saturation, and catalytic efficiency of enzymes.