BIO 361 Study Guide - Midterm Guide: Signal Transduction, Redox, Bound 2
3 Feb 2021
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Describe how k d can be used to describe the affinity of protein-ligand complexes. K d is the concentration of ligand needed to fill 50% of binding sites with enzymes. Means less ligand needed to reach 50% binding. Explain how the structure of myoglobin and hemoglobin promote oxygen binding. Tertiary structures of myoglobin and hemoglobin are almost identical. Hemoglobin and myoglobin use the same mechanics to bind to o 2 (heme) Protein groups bound to heme bind to o 2 well. Nonprotein group which binds irreversibly to a protein and imparts additional functions onto it. 1 molecule heme can bind to 1 molecule o 2. Free heme binds to co with greater affinity than o 2. Myoglobin structure positioned to form h-bond with o 2 only if tilted. O 2 binds tilted b/c of its structure while co binds straight. Storage protein, so it holds onto o 2 tightly at low concentrations.
