BCH 2333 Lecture 12: Lecture 13 - Cooperativity and enzyme kinetics
22 Mar 2017
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This also includes enzyme inhibition but it probably won"t be on midterm. Protein can exist in 2 states which are in equilibrium. Substrate can bind in 2 different equilibrium structures. First ligand binds to the to since it to is in higher concentration compared to ro. T1 is in equilibrium with r1, so ligand number 2 binds #1 state. Back and forth binding ending up with the last all bonded state because of the equilibrium concentrations. Subunites of mutimeric proteins have 2 conformational states. T and r, low and high affinity states. Conformational change of one subunit decreases the energy for conformation change in other subunits. Subunit -l complex causes conformational change to a high affinity state. Will induce conformational change in adjacent protein subunit. On binds first, the next subunits are more likely to bind. Binding of ligand to low affinity t state induces a conformational change to an intermediate affinity state.
