What is an example where molecules or aroma within a cell physically overcome some barrier to their reaction going forward thag is exergonic one? (hint: think about what a catalyst physically does during a reaction).
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What is an example where molecules or aroma within a cell physically overcome some barrier to their reaction going forward thag is exergonic one? (hint: think about what a catalyst physically does during a reaction).
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- Consider a reaction in which reactants X and Y combine to form the product Z. The diagram below compares the reaction coordinates for the catalyzed and uncatalyzed pathways of this reaction. B. X+Y Reaction Coordinate What does letter B represent? O Letter B represents the activation energy of the uncatalyzed reaction pathway. Letter B represents the energy difference between the reactants and products for the uncatalyzed pathway. O Letter B represents the activation energy of the catalyzed reaction pathway. Letter B represents the energy difference between the reactants and products for the catalyzed pathway. EnergyAn enzyme has a single active site at which it can bind and hydrolyze either X or Y but the enzyme cannot bind X and Y at the same time. Which of the following statements are TRUE? Multiple answers: Multiple answers are accepted for this question Select one or more answers and submit. For keyboard navigation. SHOW MORE The Km for X will be affected if Y is present in the reaction mixture. a Y is a competitive inhibitor of X. The Km for X will increase. d The Vmax for X will be affected if Y is present in the reaction mixture. pH dependence of Vmax reflects the ionization state of catalytic site residues. e Consider the following: X and Y are methanol (poisonous) and ethanol respectively. If the Km for X= 0.01 M and the Km f for Y = 0.001 M then 0.01 M Y is 10 times the concentration of Y required for 0.5 Vmax. Addition of an enzyme to a chemical reaction increases the ratio of products to reactants (Ken). A mutation in the active site of an enzyme resulting in a large increase in…Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pes
- Use the energy graph shown here to define and explain the importance of the following four terms. You must refer to the parts of the graph as examples. Don't forget to define AND explain all four terms. - uncatalyzed catalyzed Reactant Product Course of Reaction A. Activation energy B. Catalysis C. Gibbs free energy D. Exergonic reactions For the toolh Energy Released Energy SuppliedIn order for the reaction rate to rise the activation energy should be Select one: O O O O a. decreased b. increased c. decreased or increased d. not changed Riboflavin gives rise to cofactors:this one represents an endothermic reaction. Things are similar: the flat line on the left (beginning of the reaction) is the total energy possessed by the reactant molecules; once again, kJ stands for energy in kiloJoules, thousands of Joules. The flat line on the right (reaction complete) is the total energy of the products. Since an endothermic reaction has a net absorption of energy (taking this extra energy from the surroundings), the products have higher energy than the reactants. Question: the energy of the reactant molecules is kJ. [to answer, simply identify the correct y-axis coordinate.] 250 200 PE (kJ) 150 100 50 Reaction pathway
- Which of the following aspects of catalysis by enzymes can NOT be explained by the Fischer Lock and Key Hypothesis? Enzymes will lower the activation energy barrier for reaction. Enzymes will specifically recognize their substrates. Appropriate substrates will bind to the enzyme to form a Michaelis complex. Enzymes have an "active site" where appropriate substrates will be bound. Two of the above cannot be explained by the Fischer "Lock and Key" Hypothesis.The line does not cross the X-axis when the Y-variable is equal to zero 1점 because * Why does this line not start exactly at (0,0)? Rate of Reaction Enzyme Concentration the low concentration of enzyme is still enough to catalyze some reaction some small amount of product can be formed even without the enzyme present some small amount of product can be formed even without any product the pH was changedWhich one of the following statements is completely TRUE? O When AG > 0, the reaction is BOTH product-favored (spontaneous) AND endergonic. When AG 0, the reaction is BOTH reactant-favored (nonspontaneous) AND endergonic. When AG > 0, the reaction is BOTH product-favored (spontaneous) AND exergonic. When AG > 0, the reaction is BOTH reactant-favored (nonspontaneous) AND exergonic. When AG < 0, the reaction is BOTH reactant-favored (nonspontaneous) AND exergonic.
- Which of the following are effects of catalyst that cause an increase in the rate of reaction? (This is a multi-select question. Select all that apply). a decrease in DG‡. an increase in DG. an increase in temperature. an increase in the energy of the molecules/ions of reactant. an increase in the number of molecules/ions of reactant with enough energy to overcome the activation energy barrier.Which of the following is not an assumption made when evaluating Michaelis Menton kinetics? the reaction is happening at body temperature the substrate is in great excess of the catalyst measurement of initial velocity of the reaction reaction conditions are occurring under steady stateWhich of the following statements is false regarding an enzyme's ability to catalyse a reaction? an enzyme provides a reaction surface and a hydrophilic environment for the reaction to take place an enzyme binds reactants such that they are positioned correctly and can attain their transition-state configurations an enzyme allows the reaction to go through a more stable transition state than would normally be the case an enzyme can weaken bonds in reactants through the binding process