Chapter 8, Problem 2
What is a transition state? a. the shape adopted by an enzyme that has an inhibitory molecule bound at its active site b. the amount of kinetic energy required for a reaction to proceed c. the intermediate complex formed as covalent bonds in the reactants are being broken and re-formed during a reaction d. the enzyme shape after binding an allosteric regulatory molecule
Video transcript
Which of the following correctly describe an exergonic reaction? Select True or False for each statement. T/F The products have lower Gibbs free energy than the reactants. T/F Activation energy is required for the reaction to proceed. T/F The products always have lower entropy than the reactants. T/F The reaction always occurs quickly.
How does pH affect enzyme-catalyzed reactions? a. Protons serve as substrates for most reactions. b. Energy stored in protons is used to drive endergonic reactions. c. Proton concentration increases the kinetic energy of the reactants, enabling them to reach their transition state. d. The concentration of protons affects an enzyme's folded structure and reactivity.
What factors determine whether a chemical reaction is spontaneous or not?
Which of the following correctly describe an active site? Select True or False for each statement. T/F It is the location in an enzyme where substrates bind. T/F It is the place where a molecule or ion binds to an inactive enzyme to induce a shape change to make it active. T/F It is the portion of an enzyme where chaperones bind to help enzymes fold. T/F It is the site on an enzyme where catalysis occurs.