BIOL 3210 Lecture Notes - Lecture 11: Uncoupling Protein, Binding Energy, Turnover Number

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26 May 2017
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Slides taken out for the exam next friday. Binding energy lowers the activation energy to make the reaction go. This energy is released when favorable reactions are made between the substrate and the enzyme. First to point out that enzymes stabilize the transition state. The transition state should be the best binding partner. Binding energy drives catalysis things want to be together. Energy is released when things come together. Specificity only the right substrate will let you go towards the transition state with a release of energy. Induced fit a precise fit that helps stabilize the transition state. Enzymes lower entropy by binding in a specific way. Desolvation water is removed when they interact. Everything we are going to talk about is exergonic. Lock and key model the lock is the enzyme and the key is the substrate. Only a correctly sized key (substrate) will fit into certain locks (enzymes). Enzymes without the cofactor is the apoenzyme.

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