Lecture 8 - Cooperativity and allostery Flashcards
If we have a protein with one binding site for a ligand, the number of ligands bound per site depends on
- Ligand concentration in solution
- Binding constant, K
The number of ligands bound per site is called the
fractional saturation (ϴ)
A binding curve for a ligand and a protein with more than one binding site is _______ shape.
sigmoidal
A binding curve for a ligand and a protein with one binding site is _______ shape.
hyperbolic
Cooperative binding
The binding of one ligand to one site increases its affinity to the next site
Cooperative binding is a property of _______ proteins
multisubunit
For cooperative binding, the first binding step corresponds to a(n) ______ in Gibbs energy
increase
Cooperativity is the key mechanism for
allosteric regulation
Allosteric regulation is
the regulation of an enzyme or protein by binding an effector molecule to a site other than the enzyme’s active site
Allosteric sites allow effectors to bind to the protein, resulting in a
conformational change
Allosteric activators are
effectors that enhance the protein’s activity
Allosteric inhibitors
effectors that decrease the protein’s activity
The approach to saturation is controlled only by the
binding constant K
Hemoglobin role
transport O2 from lungs to tissues
Myoglobin role
O2 storage protein