1. What is the relationship between energy content ofa molecule and stability? Why is it, that all biological molecules are relatively stable? ( pt) 2. Why do even exergonic biological reactions almost always require a catalyst? What does this catalyst do? (1 point) 3. In a particular reaction X is converted to Y, with a free energy o contains more energy, X or Y? Which molecule is more stable? At equilibrium, will the concentration of X or Y be higher? If more “X” is added, will the reaction go to the left or right? (1 pts) f-5.5 kcal/mole. Which molecule 4. Trypsin is an enzyme that aids in protein digestion. In the binding pocket (active site) of the enzyme, there is an Aspartic Acid residue. How do you think changing this amino acid to Lysine would affect the enzyme’s activity? How would it affect enzyme affinity and turnover rate for its substrate? (see Fig 3.2 for amino acid R group structures) (2 points) s. What exactly is the transition state and how does an enzyme help move a substrate to the transition state? What is the energy of the transition state molecule relative to that of substrate or product? What is it stability relative to that of substrate & product? Why is this important? (2 pts) 6. A particular biological molecule has a molecular weight of 400. How many grams of this substance are needed to have 1 mole of this substance? Suppose you could burn exactly 1 mole of this molecule and you found that the released heat caused the temperature of 1 kg of water to rise by 10C. How many calories are in one mole of this substance? 2 pt) 7. In a particular reaction, Substance “X” is converted to substance “Y” with a Delta G of -12 Kcal/mole. In an experiment, both “X” and “Y” are placed in a flask with the necessary enzyme. After equilibrium is reached: will the concentration of X be greater, less or equal to Y? ( pt)