Cooperativity (video) | Enzyme kinetics | Khan Academy
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Cooperativity (video) | Enzyme kinetics | Khan Academy
Explore the intriguing world of enzyme kinetics and cooperative binding. Delve into the two-step process of enzyme catalysis, the Michaelis Menten equation, and the effects of increasing substrate concentration. Understand the concept of multiple substrate binding sites and the three types of cooperativity: Positive, Negative, and Non ...
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SOLVED:A dimeric enzyme shows positive cooperativity for substrate binding. Cooperativity can be described by the concerted model. The enzyme exists in two conformations that are in equilibrium: either both protomers are in the T state that does not bind substrate, or both protomers are in the R state that binds substrates with high affinity (dissociation constant KS ). The equilibrium constant for the conformational equilibrium is L=[T]0 /[R]0. The rate of product formation is kp (for each acti
SOLVED:A dimeric enzyme shows positive cooperativity for substrate binding. Cooperativity can be described by the concerted model. The enzyme exists in two conformations that are in equilibrium: either both protomers are in the T state that does not bind substrate, or both protomers are in the R state that binds substrates with high affinity (dissociation constant KS ). The equilibrium constant for the conformational equilibrium is L=[T]0 /[R]0. The rate of product formation is kp (for each acti
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