BIOC 2300 Lecture Notes - Lecture 10: Enthalpy, Gibbs Free Energy, Epitope
29 Jan 2019
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Document Summary
Although it forms hydrogen bonds, there are lots of intermolecular interactions. Antibody-binding epitope there are key different interactions that occur. In general, it focuses on the antibody complementary. Hydrophobic regions of the epitope are recognized by the hydrophobic region on the anitibody. Close approach of two atoms: the same forces drive both the folding of molecules and the associations between them. Stable energy, and repulsion occurs where atoms tend to clash together drives the folding of the molecules. Quantitative treatment of 1:1 binding: for a typical 1:1 intermolecular reaction: L = binding ligand (ligand or another protein) P = host protein (typically a protein at lower concentration: at equilibrium, rearranges to: Note: a small kd means that the complex is high affinity! We can determine by measuring rates or concentrations: fraction bound , the dissociation constant (kd) is a measurement of the affinity of two molecules for each other.
