MEGA EXAM SOCIAL STUDIES LATEST UPDATED REAL 2025
FINAL EXAM WITH COMPLETE DETAILED QUESTIONS AND
CORRECT VERIFIED ANSWERS ALREADY A+ GRADED
A variety of factors influence enzyme activity. Substances that bind to the enzyme and interfere with
substrate binding or catalysis are inhibitors. Identify the type of inhibition associated with each of the
descriptions and examples by classifying each statement as irreversible, competitive, or mixed
inhibition.
ANSWER-Irreversible inhibition
inhibitor may permanently modify an enzyme
DIPFDIPF permanently modifies the hydroxyl group of a Ser residue at the active site
Competitive inhibition
ANSWER-inhibitor binds reversibly to an enzyme's active site
malonate, which resembles succinate, binds to the succinate dehydrogenase active site
Mixed inhibition
ANSWER-inhibitor binds to an enzyme at a site other than the active site
the Al+3Al3+ ion binds to acetylcholinesterase or to the acetylcholinesterase‑substrate complex
Classify each phrase as describing a competitive inhibitor, uncompetitive inhibitor, or mixed (mixed
noncompetitive) inhibitor. Note that 𝐾mKm refers to apparent 𝐾mKm .
ANSWER-Competitive inhibitor
structurally similar to substrate
when present, 𝐾mKm of enzyme will increase
,prevents substrate from binding enzyme
Uncompetitive inhibitor
ANSWER-when present, 𝐾mKm of enzyme will decrease
binds enzyme-substrate complex only
Mixed inhibitor
ANSWER-binds either enzyme or enzyme-substrate complex
when present, 𝐾mKm of enzyme will either increase or decrease
A variety of factors influence enzyme activity. Substances that bind to the enzyme and interfere with
substrate binding or catalysis are inhibitors. Identify the type of inhibition associated with each
description and example by classifying them into the appropriate category.
ANSWER-Irreversible inhibition
inhibitor may permanently modify an enzyme
DIPF permanently modifies the hydroxyl group of a SerSer residue at the active site
Competitive inhibition
ANSWER-inhibitor binds reversibly to an enzyme's active site
a transition state analog binds reversibly to isomerase
Noncompetitive inhibition
ANSWER-inhibitor binds to an enzyme at a site other than the active site
the Al3+Al3+ ion binds to acetylcholinesterase or to the acetylcholinesterase‑substrate complex
,In the lungs, oxygen diffuses into the blood and is loaded onto hemoglobin for transport. In the tissues,
oxygen is unloaded from hemoglobin and diffuses from the blood into nearby cells.
What drives the diffusion of oxygen?
ANSWER-pressure of oxygen
Determine which statements apply to hemoglobin, myoglobin, or neither.
ANSWER-Hemoglobin
The oxygen dissociation curve is sigmoidal in shape ("S"‑shaped).
As oxygen binds to this molecule the shape of the molecule changes, enhancing further oxygen binding.
The binding pattern for this molecule is considered cooperative.
This molecule delivers oxygen more efficiently to tissues.
Myoglobin
The oxygen dissociation curve is hyperbolic in shape.
This molecule has a greater affinity for oxygen.
Neither
Oxygen binds irreversibly to this molecule.
Carbon monoxide binds at an allosteric site, lowering oxygen binding affinity.
The graph shows the oxygen‑binding curves for myoglobin and hemoglobin. Label the graph and answer
the questions.
Use the curves to determine the partial pressure of oxygen at 50% saturation for hemoglobin and
myoglobin.
ANSWER-myoglobin 𝑃50=P50=
, hemoglobin 𝑃50=P50=
Which protein has a higher affinity for oxygen?
ANSWER-graph lecture 9 question 3
myoglobin 𝑃50= 30
hemoglobin 𝑃50= 2
myoglobin
Complete the sentences about heme.
Some terms will not be used.
ANSWER-The prosthetic group of hemoglobin and myoglobin is heme.
The organic ring component of heme is porphyrin.
Under normal conditions, the central atom of heme is Fe2+.
In deoxyhemeoglobin the central iron atom is displaced 0.4 Å out of the plane of the porphyrin ring
system.
The central atom has 6 bonds: to 4 nitrogen atoms in the porphyrin, one to a histadine residue, and one
to oxygen.
Select all statements that correctly describe hemoglobin and myoglobin structure.
ANSWER-Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a
central iron (Fe)(Fe) atom.
By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of
the iron..
Hemoglobin is a heterotetramer, whereas myoglobin is a monomer.Molecular oxygen binds reversibly
to the Fe(II)Fe(II) atom in heme.
FINAL EXAM WITH COMPLETE DETAILED QUESTIONS AND
CORRECT VERIFIED ANSWERS ALREADY A+ GRADED
A variety of factors influence enzyme activity. Substances that bind to the enzyme and interfere with
substrate binding or catalysis are inhibitors. Identify the type of inhibition associated with each of the
descriptions and examples by classifying each statement as irreversible, competitive, or mixed
inhibition.
ANSWER-Irreversible inhibition
inhibitor may permanently modify an enzyme
DIPFDIPF permanently modifies the hydroxyl group of a Ser residue at the active site
Competitive inhibition
ANSWER-inhibitor binds reversibly to an enzyme's active site
malonate, which resembles succinate, binds to the succinate dehydrogenase active site
Mixed inhibition
ANSWER-inhibitor binds to an enzyme at a site other than the active site
the Al+3Al3+ ion binds to acetylcholinesterase or to the acetylcholinesterase‑substrate complex
Classify each phrase as describing a competitive inhibitor, uncompetitive inhibitor, or mixed (mixed
noncompetitive) inhibitor. Note that 𝐾mKm refers to apparent 𝐾mKm .
ANSWER-Competitive inhibitor
structurally similar to substrate
when present, 𝐾mKm of enzyme will increase
,prevents substrate from binding enzyme
Uncompetitive inhibitor
ANSWER-when present, 𝐾mKm of enzyme will decrease
binds enzyme-substrate complex only
Mixed inhibitor
ANSWER-binds either enzyme or enzyme-substrate complex
when present, 𝐾mKm of enzyme will either increase or decrease
A variety of factors influence enzyme activity. Substances that bind to the enzyme and interfere with
substrate binding or catalysis are inhibitors. Identify the type of inhibition associated with each
description and example by classifying them into the appropriate category.
ANSWER-Irreversible inhibition
inhibitor may permanently modify an enzyme
DIPF permanently modifies the hydroxyl group of a SerSer residue at the active site
Competitive inhibition
ANSWER-inhibitor binds reversibly to an enzyme's active site
a transition state analog binds reversibly to isomerase
Noncompetitive inhibition
ANSWER-inhibitor binds to an enzyme at a site other than the active site
the Al3+Al3+ ion binds to acetylcholinesterase or to the acetylcholinesterase‑substrate complex
,In the lungs, oxygen diffuses into the blood and is loaded onto hemoglobin for transport. In the tissues,
oxygen is unloaded from hemoglobin and diffuses from the blood into nearby cells.
What drives the diffusion of oxygen?
ANSWER-pressure of oxygen
Determine which statements apply to hemoglobin, myoglobin, or neither.
ANSWER-Hemoglobin
The oxygen dissociation curve is sigmoidal in shape ("S"‑shaped).
As oxygen binds to this molecule the shape of the molecule changes, enhancing further oxygen binding.
The binding pattern for this molecule is considered cooperative.
This molecule delivers oxygen more efficiently to tissues.
Myoglobin
The oxygen dissociation curve is hyperbolic in shape.
This molecule has a greater affinity for oxygen.
Neither
Oxygen binds irreversibly to this molecule.
Carbon monoxide binds at an allosteric site, lowering oxygen binding affinity.
The graph shows the oxygen‑binding curves for myoglobin and hemoglobin. Label the graph and answer
the questions.
Use the curves to determine the partial pressure of oxygen at 50% saturation for hemoglobin and
myoglobin.
ANSWER-myoglobin 𝑃50=P50=
, hemoglobin 𝑃50=P50=
Which protein has a higher affinity for oxygen?
ANSWER-graph lecture 9 question 3
myoglobin 𝑃50= 30
hemoglobin 𝑃50= 2
myoglobin
Complete the sentences about heme.
Some terms will not be used.
ANSWER-The prosthetic group of hemoglobin and myoglobin is heme.
The organic ring component of heme is porphyrin.
Under normal conditions, the central atom of heme is Fe2+.
In deoxyhemeoglobin the central iron atom is displaced 0.4 Å out of the plane of the porphyrin ring
system.
The central atom has 6 bonds: to 4 nitrogen atoms in the porphyrin, one to a histadine residue, and one
to oxygen.
Select all statements that correctly describe hemoglobin and myoglobin structure.
ANSWER-Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a
central iron (Fe)(Fe) atom.
By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of
the iron..
Hemoglobin is a heterotetramer, whereas myoglobin is a monomer.Molecular oxygen binds reversibly
to the Fe(II)Fe(II) atom in heme.
