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Protein-Ligand Binding Overview

Sep 13, 2025

Overview

This lecture covers how proteins interact with ligands, the chemical nature of these interactions, and how to measure and interpret binding affinity using the dissociation constant (Kd).

Protein-Ligand Interactions

  • Proteins bind ligands, which can be any molecule: another protein, DNA, nucleotides, etc.
  • Binding usually involves a specific binding pocket or interface on the protein.
  • Not all interactions are with a "pocket"; some involve flat binding surfaces.
  • Protein-ligand interactions are typically mediated by non-covalent bonds (weaker and reversible).

Non-Covalent Bonds and Affinity

  • Non-covalent bonds include hydrogen bonds, ionic bonds, and van der Waals interactions.
  • Binding specificity depends on shape compatibility and chemical properties of side chains (R groups) in the binding site.
  • The fit between protein and ligand (three-dimensional and chemical) determines the number and strength of bonds.
  • More and stronger non-covalent bonds result in higher binding affinity (longer binding time).

Measuring and Describing Affinity

  • Affinity describes how tightly a protein binds its ligand; higher affinity means longer binding.
  • Affinity is measured using the dissociation constant (Kd).
  • Kd is found by titrating ligand into a fixed protein concentration and identifying the ligand concentration where half the protein is bound.
  • A lower Kd means higher affinity; a higher Kd means lower affinity.
  • Kd is expressed in molar units (commonly micromolar or nanomolar in cells).
  • The relationship is inverse: high affinity = low Kd, low affinity = high Kd.

Key Terms & Definitions

  • Ligand — Any molecule that binds to a protein (could be small or large).
  • Binding Pocket — The specific region on a protein where a ligand binds.
  • Non-Covalent Bond — A chemical bond that does not involve sharing electrons; weaker than covalent bonds.
  • Affinity — The strength or tightness of the protein-ligand interaction.
  • Dissociation Constant (Kd) — The concentration of ligand at which half the protein is bound; lower values indicate higher affinity.

Action Items / Next Steps

  • Watch movie 2.4 in the movies folder to see molecular interactions.
  • Review provided readings on protein-ligand interactions and Kd.
  • Prepare for next lecture on enzyme function.