Quick question of clarification,
If a particular receptor has a dissociation constant (Kd) of 50nM for instance. That means that the receptor is half bound by ligand when the concentration of the ligand is 50nM.
To fully saturate a receptor, would one use twice as much ligand? 100nM in this case?
Thanks for your help with this….
All the best 🙂
not really, it’s similar as Michaelis with enzymes, so you won’t get twice so much bound ligands 😉
Usually, 10× more is taken to fully saturate 😉