1. A ligand binds more tightly to the folded state (N) of a protein than to the unfolded state (U). Show that the ligand stabilizes the protein and calculate by how much (DDGfold = ?)
1. A ligand binds more tightly to the folded state (N) of a protein than to the unfolded state (U). Show that the ligand stabilizes the protein and calculate by how much (DDGfold = ?)
2. An enzyme E binds a substrate S and a cofactor C. The equilibrium dissociation constant Kd,S of the enzyme-substrate complex ES is 1 μM, for EC it is 10 μM. When the cofactor C is present, Kd,s’ is decreased to 0.1 μM. What is the value for the dissociation constant Kd,C’ of the enzyme-cofactor complexing the presence of substrate S? Calculate the interaction energy DDGint for cofactor and substrate binding.
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Proteins are polymers of amino acids which are folded in three dimensional structure by both covalent and non-covalent interactions. Ligands are molecules that influence the function of protein (proteins such as an enzyme, receptor, etc). Thus, ligand produces a signal by binding to the target proteins. Ligands can bind strongly to only folded protein and the unfolded protein will not be able to recognize the ligand. Ligand also stabilizes the protein.
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