3. The crystal structure visualizations below show examples of substrates or inhibitors within the binding sites of enzy

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3 The Crystal Structure Visualizations Below Show Examples Of Substrates Or Inhibitors Within The Binding Sites Of Enzy 1 (56.48 KiB) Viewed 83 times

3. The crystal structure visualizations below show examples of substrates or inhibitors within the binding sites of enzymes. Examine these carefully, and draw each small molecule depicted therein. Account for stereochemistry whenever appropriate. (Note: red oxygen, blue - nitrogen, lime green=fluorine, yellow - sulfur, dark green carbon) Shows I *Note: lime green in this structure denotes chlorine, 4. In the active site of a zinc protease, how does the zinc cation affect the pk of the associated water molecule? Explain the chemical basis for this change, and why this is important to the function of the enzyme 5. Aspartyl proteases contain two Asp residues that participate in acid-base catalysis for the hydrolysis of peptide bonds. How does the hydrophobic pocket enable one of the Asp residue side chains to remain in the protonated (and thus nonlonized) state even at physiologic pH? Explain in terms of the intermolecular interactions involved