Protein Function Flashcards
What is a ligand?
any molecule that a protein can bind to in a reversible manner, Typically a smaller molecule
What is a binding site?
A site on a protein where ligand binds; very specific!
What does induced fit mean?
When both the ligand and the protein can change their conformations upon binding; makes binding site more complementary to ligand.
What does affinity mean?
It is a measure of how tightly a protein P binds to ligand L.
How is affinity measured?
Affinity is quantitatively expressed as a dissociation constant Kd, which is simply an equilibrium constant for the dissociation reaction. (Lower the Kd the higher the binding)
Equation for Kd
Kd = [P] [L] / [PL]
How would a protein have multiple binding sites?
If it has multiple subunits.
What is cooperatively?
An interaction is cooperative if the binding of one ligand molecule affects the affinity of another ligand molecule on the same protein. It requires multiple domains or subunits.
Positive cooperativity
occurs when the binding of a ligand increases the binding affinity of subsequent ligands.
Negative cooperativity
occurs when the binding of a ligand decreases the binding affinity of subsequent ligands.
What is an allosteric protein?
When binding of one ligand (the effector) affects the binding of another ligand to a different binding site on the same protein. DOES NOT ALWAYS REQUIRE MULTIPLE SUBUNITS!
Myoglobin
Contains 1 subunit. Used for O2 storage. Contains 1 heme group.
Hemoglobin
Contains 4 subunits - 2 alpha and 2 beta (multiple hetero binding sites). Used for O2 transport. Contains 4 heme groups (can bind 4 oxygens).