Part E A rate enhancement of 100 requires that the enzyme bind its transition state complex with higher affinity than its substrate. Using the Arrhenius equation, shown before this part, find AAGEat for a rate enhancement of 106 at 298 K. Express AAGEat in kJ/mol to three significant figures. 34.2 kJ/mol Submit Previous Answers ✓ Correct AAG is the difference in free energy of the transition state between the uncatalyzed and catalyzed reaction. Since the catalyzed reaction has a lower activation energy at the transition state, it is expected to also have a more favorable AG value.

Part F Below is a table of common intermolecular forces found in the active sites of enzymes: kJ/mol Hydrogen bonds 10 to 40 Dipole-dipole interactions 5 to 25 Dispersion forces 0.5 to 40 Using your value from the previous question, determine how many H bonds or dipole interactions would be required to achieve a rate enhancement of 10º. Match the values in the left column to the appropriate blanks in the sentences on the right. Reset Help 1.37 to 3.42 To achieve a rate enhancement of 100, a total of hydrogen bonds or 0.86 to 68.4 dipole interactions would be required. 1.37 to 6.84 0.86 to 3.42 3.42 to 68.4 Submit Request Answer