BIOL-1100 Lecture Notes - Lecture 16: Oxidative Phosphorylation, Dissociation Constant, Reaction Rate Constant
28 Jun 2016
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Document Summary
Globular proteins store ions and molecules, transport ions and molecules, defend against pathogens, contribute to muscle contraction, biological catalysis. Binding is calculated through ka and kd. Ka=association rate constant; if ka increases increases. Kd= dissociation rate constant, concentration of ligand when sites are taken; kd increases decreases. As [l] increases increases, [pl] increases increases. Complementary: proteins are specific because ligand and binding site complement each other. Induced fit: conformational changes that occur once ligand binds, tighter binding. Co is highly toxic because it blocks the function of myoglobin, hemoglobin, and mitochondrial cytochromes involved in oxidative phosphorylation. The protein pocket in myoglobin and hemoglobin decreases affinity for co. Myglobin is not a good transporter of o2 but is good for storage because heme has such a high affinity for o2. Hill plots of cooperativity slope= hill coefficient (degree of cooperativity) Different slopes at different concentrations: n=1: no cooperativity, n<1: negative cooperativity, n>1: positive cooperativity.
