Is the bolded statement TRUE or FALSE? In chapter 7 we discu…

Is the bolded statement TRUE or FALSE? In chapter 7 we discussed major concepts related to the kinetics of an enzymatically catalyzed reaction.  Given this classify the following as true or false. 31. Saturating conditions result in [ES] approximately equal to [ET].  32. The kcat is the largest rate constant of any of the steps employed by the enzyme. 33. Loss of an ionic bond, due to mutation of the enzyme, between the enzyme active site and the substrate will lead to a depression (making it smaller) in the Km. 34. An enzyme with a larger kcat will always be a more “efficient” enzyme, in all conditions, than the one with the small kcat. 35. If all of an enzyme is in the ES form, the enzyme will obtain its Vmax.

The current level of S&P 500 index is 1300. The annual risk-…

The current level of S&P 500 index is 1300. The annual risk-free rate is 6%, and the annual dividend yield is 1%. Jane decides to enter to long one futures contract on S&P 500 that matures in 6 months. The multiplier of the futures contract is $250. The initial margin requirement is 10% of the contract value. Assuming that the futures position is priced efficiently, how much should Jane deposit in her account as the 10% initial margin? (Hint: Current level ≠ Futures price)

Is the bolded statement TRUE or FALSE? In class we spent som…

Is the bolded statement TRUE or FALSE? In class we spent some time on the design of the oxygen-binding pocket of both Hb and Mb to illustrate the structural functional relationship within these proteins.  The distal His (His E7), as discussed, forms the top portion of the oxygen-binding pocket and the proximal His (His F8), forms the bottom portion and a covalent bond to the heme.  We then moved into the allosteric behavior of Hb.  Given these topics which of the following statement(s) is (are) true? 56. BPG shifts the equilibrium of Hb’s conformation toward the “T”-state.57. Replacement of the distal His with a Gly side chain would result in a Mb or Hb protein with a decreased affinity for oxygen. 58. Replacement of the distal His with a Trp side chain would result in a Mb or Hb protein with a decreased affinity for carbon monoxide. 59. The distal His can form a hydrogen bond to both oxygen and carbon monoxide.60. If a molecule that binds to Hb causing a shift of Hb’s conformation toward the R-state, the Kd of Hb for oxygen will decrease.