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Unformatted text preview: 1. A small molecule that DECREASES the activity of an enzyme by binding to the enzyme and altering the three dimensional structure thereby decreasing substrate binding to the active site is termed a(n): A) alternative activator B) competitive inhibitor C) allosteric inhibitor D) competitive activator E) transition‐state analog 2. Which of the following agents and/or procedures would interfere with or disrupt the primary structure of a protein in solution at pH 7.0? A) Addition of a strong detergent causing protein unfolding B) A large increase in ionic strength of the solution C) Addition of an enzyme which hydrolyzes peptide bonds D) A and B E) A, B and C 3. The graph below describes the reaction coordinates for the conversion of a particular substrate to product. This reaction proceeds very slowly unless the proper enzyme is added to the reaction. The addition of enzyme to this reaction will speed up the reaction by: A) B) C) D) E) increasing the ground state free energy of the substrate decreasing the ground state free energy of the product decreasing the energy difference between the substrate and the product (∆G’o) changing the equilibrium constant lowering the activation energy (∆Gact) 4. An allosteric interaction between a ligand and a protein is one in which: A) two different ligands can bind to the same binding site B) the binding of the ligand to the protein is covalent C) multiple molecules of the same ligand can bind to the same binding site D) the binding of a molecule to its binding site affects the binding of an additional molecule to the same site E) the binding of a molecule to a binding site affects the binding properties of another site on the protein 5. From the following titration curve of aspartic acid 9.82 3.86 2.10 The isoelectric point is: A) 2.10 B) 2.98 C) 3.86 D) 6.84 E) 9.82 At what pH is the following reaction occurring? NH3‐ + OH‐ → NH2‐ + H2O A) 2.10 B) 2.98 C) 3.86 D) 6.84 E) 9.82 ...
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This note was uploaded on 12/11/2010 for the course BIOC 423 taught by Professor Robert during the Fall '10 term at New Mexico.
- Fall '10