Question 1
Histidine has 3 ionizable groups.
The pKa of the alpha COOH is 1.8; the pKa on the R group is 6.0; the pka on
the alpha-amino group is 9.3.
At a pH of 5, what would the net charge on histidine be?
Selected Answer:
+1
Correct Answer:
+1
Response
Feedback: Calculate the net charge on a molecule using the
pKa(s) of ionizable group
See figure 6.8
Question 2
The Lineweaver - Burk plot above illustrates the kinetics of a reaction with and
without the addition of an inhibitor. Which of the following statements is
consistent with this graph?
Selected
Answer: The red line illustrates the change in activity with the addition of a
competitive inhibitor
, Correct
Answer: The red line illustrates the change in activity with the addition of a
competitive inhibitor
Response
Feedback: Evaluate the change in the Km or Vmax of an enzyme with
the addition of a competitive or noncompetitive inhibitor.
(Figure 9.14)
Question 3
What is the [H+] concentration in a 0.001 M = 10-3 M solution of NaOH.
(10-14 = [H+] [OH-])
Selected Answer:
10-11 M
Correct Answer:
10-11 M
Response
Feedback: Page 44. Section II
Calculate the [OH] OR [H+] concentration if given the
molarity of a solution.
Question 4
, With respect to Michaelis-Menten kinetics, the addition of a noncompetitive
inhibitor to a reaction would result in which of the following?
Selected Answer:
An increase in Km and no change in Vmax
Correct Answer:
No change in Km and a decrease in Vmax
Question 5
The concentration of an enzyme will impact the rate of an overall reaction.
Which of the following will lead to an overall decrease in enzyme
concentration?
Selected Answer:
Increased enzyme degradation
Correct Answer:
Increased enzyme degradation
Response
Feedback: Apply how changes in enzyme concentration can be
controlled by changes in the rate of transcription or
degradation
Question 6
Initiation of gene transcription in both pro and eukaryotes generally involves
Histidine has 3 ionizable groups.
The pKa of the alpha COOH is 1.8; the pKa on the R group is 6.0; the pka on
the alpha-amino group is 9.3.
At a pH of 5, what would the net charge on histidine be?
Selected Answer:
+1
Correct Answer:
+1
Response
Feedback: Calculate the net charge on a molecule using the
pKa(s) of ionizable group
See figure 6.8
Question 2
The Lineweaver - Burk plot above illustrates the kinetics of a reaction with and
without the addition of an inhibitor. Which of the following statements is
consistent with this graph?
Selected
Answer: The red line illustrates the change in activity with the addition of a
competitive inhibitor
, Correct
Answer: The red line illustrates the change in activity with the addition of a
competitive inhibitor
Response
Feedback: Evaluate the change in the Km or Vmax of an enzyme with
the addition of a competitive or noncompetitive inhibitor.
(Figure 9.14)
Question 3
What is the [H+] concentration in a 0.001 M = 10-3 M solution of NaOH.
(10-14 = [H+] [OH-])
Selected Answer:
10-11 M
Correct Answer:
10-11 M
Response
Feedback: Page 44. Section II
Calculate the [OH] OR [H+] concentration if given the
molarity of a solution.
Question 4
, With respect to Michaelis-Menten kinetics, the addition of a noncompetitive
inhibitor to a reaction would result in which of the following?
Selected Answer:
An increase in Km and no change in Vmax
Correct Answer:
No change in Km and a decrease in Vmax
Question 5
The concentration of an enzyme will impact the rate of an overall reaction.
Which of the following will lead to an overall decrease in enzyme
concentration?
Selected Answer:
Increased enzyme degradation
Correct Answer:
Increased enzyme degradation
Response
Feedback: Apply how changes in enzyme concentration can be
controlled by changes in the rate of transcription or
degradation
Question 6
Initiation of gene transcription in both pro and eukaryotes generally involves
