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One between the enzyme and the substrate. way the enzyme-bound states are stabil

ID: 150117 • Letter: O

Question

One between the enzyme and the substrate. way the enzyme-bound states are stabilized is through formation of non-covalent interactions 11. Compare the magnitude of AGes and A Ges. Which form of the substrate does the enzyme bind best? How do you know? 12. As a group, develop a summary statement about the source of the free energy stabilization for the enzyme-transition state complex. Consider the change in enthalpy (energy associated with non- covalent interactions) when non-covalent interactions (very weak "bonds") are formed. 13. Suppose a second enzyme binds the substrate even more tightly than the enzyme shown in model 1 (the E S complex is more stable than the one shown in graph B). Draw this new E S complex on graph B. What happens to the magnitude of the activation energy, AGaa 14. Suppose a third enzyme binds the transition state even more tightly than the enzyme diagramed in model 2. What happens to the magnitude of the activation energy, AGact

Explanation / Answer

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11. delGES < del GES*.

Enzyme binds best to substrate in the S form rather than S* form which is evidenced by the lower free energy levels (indicating higher stability of enzyme substrate complex) of E+S as compared to E+S*.

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