BCHS 3304 Final | Questions with 100% Verified Answers |
Latest Update
Question:
An enzyme cannot make a rxn thermodynamically favorable
Answer:
True
Question:
Phase 2 clinical trails are focused on evaluating the safety of new drug candidates
Answer:
False
Question:
In the rxn coordinate graph showing below, which location(s) is (are) intermediate states?
Answer:
None of the above (C&E)
Question:
In the presence of a competitive inhibitor at [I] = 3 mM, the apparent Km is three times the KM for
the uninhibited rxn. What is K1?
Answer:
1.5 mM
Question:
The role of water in the lysozyme active site is to
Answer:
Regenerate the active form of the catalytic residues at the active site
Question:
A first order rxn has a t1/2 of 20 mins. What is the reaction rate constant k?
Answer:
0.0035 min-1
Question:
In a serine protease enzyme, the catalytic triad drawing in the order of the "proton shuttle network"
is
Answer:
Ser-His-Asp
, Question:
For the elementary rxn A + B ->P, the correct rate equation and reaction order are
Answer:
v=kAB, it is a second order rxn
Question:
Which of the following types of inhibition does the figure below reflect?
Answer:
Uncompetitive
Question:
Which of the following is not true about enzymes?
Answer:
Enzymes catalyze rxns in the forward direction only
Question:
The length of an alpha helix of 20 AA residues is
Answer:
30 A
Question:
Which residue in the seven-residue repeat (abcdefg) of the alpha-keratin helical wheel provide a
hydrophobic interaction to associate two coiled coils?
Answer:
a, d
Question:
The GFP structure is shown below. The major motif in this protein is
Answer:
beta sheets
Question:
The following figure showed the binding curves of myoglobin, stripped hemoglobin, adult
hemoglobin in whole blood at conditions of (normal, elevated CO2, elevated area). Curve a is
hyperbolic and the others are sigmoidal. The binding curve in whole blood is d. The binding curves
for myoglobin, whole blood w/ elevated CO2, and whole blood in elevated area are:
Answer:
a-e-f
Latest Update
Question:
An enzyme cannot make a rxn thermodynamically favorable
Answer:
True
Question:
Phase 2 clinical trails are focused on evaluating the safety of new drug candidates
Answer:
False
Question:
In the rxn coordinate graph showing below, which location(s) is (are) intermediate states?
Answer:
None of the above (C&E)
Question:
In the presence of a competitive inhibitor at [I] = 3 mM, the apparent Km is three times the KM for
the uninhibited rxn. What is K1?
Answer:
1.5 mM
Question:
The role of water in the lysozyme active site is to
Answer:
Regenerate the active form of the catalytic residues at the active site
Question:
A first order rxn has a t1/2 of 20 mins. What is the reaction rate constant k?
Answer:
0.0035 min-1
Question:
In a serine protease enzyme, the catalytic triad drawing in the order of the "proton shuttle network"
is
Answer:
Ser-His-Asp
, Question:
For the elementary rxn A + B ->P, the correct rate equation and reaction order are
Answer:
v=kAB, it is a second order rxn
Question:
Which of the following types of inhibition does the figure below reflect?
Answer:
Uncompetitive
Question:
Which of the following is not true about enzymes?
Answer:
Enzymes catalyze rxns in the forward direction only
Question:
The length of an alpha helix of 20 AA residues is
Answer:
30 A
Question:
Which residue in the seven-residue repeat (abcdefg) of the alpha-keratin helical wheel provide a
hydrophobic interaction to associate two coiled coils?
Answer:
a, d
Question:
The GFP structure is shown below. The major motif in this protein is
Answer:
beta sheets
Question:
The following figure showed the binding curves of myoglobin, stripped hemoglobin, adult
hemoglobin in whole blood at conditions of (normal, elevated CO2, elevated area). Curve a is
hyperbolic and the others are sigmoidal. The binding curve in whole blood is d. The binding curves
for myoglobin, whole blood w/ elevated CO2, and whole blood in elevated area are:
Answer:
a-e-f
