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Biological Chemistry
HW 4-7, Clicker Qs, Quiz Qs
| Question | Answer |
|---|---|
| List the intermolecular interactions that would be responsible for the reversible ligand-protein binding. | |
| Briefly, how is the in silico docking experiment done? | |
| Relationship between Affinity and Dissociation Constant Protein A has a binding site for ligand X with a ðūd of 3.0x10^-7 M. Protein B has a binding site for ligand X with a Kd of 4.0x10^-8 M. Calculate the Ka of each protein and why? | |
| Would this situation produce a Hill plot with ðH<1.0? Explain your reasoning. --The protein has multiple subunits, each with a single ligand-binding site. Ligand binding to one site decreases the binding affinity of other sites for the ligand. | |
| Modeling Apparent Negative Cooperativity: Which of these situations would produce a Hill plot with ðH<1.0? Explain your reasoning. --The protein is a single polypeptide with two ligand-binding sites, each having a different affinity for the ligand. | |
| Would this situation produce a Hill plot with ðH<1.0 and why? --The protein is a single polypeptide with a single ligand-binding site. As purified, the protein preparation is heterogeneous, containing some protein molecules that are partially denatured | |
| Would this situation produce a Hill plot with ðH<1.0 and why? The protein has multiple subunits, each with a single ligand-binding site. Ligands bind independently to each site, do not affect the binding affinity of other sites, and bind with identical |