Deck 5: Protein Function

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Question
A prosthetic group of a protein is a non-protein structure that is:

A)a ligand of the protein.
B)a part of the secondary structure of the protein.
C)a substrate of the protein.
D)permanently associated with the protein.
E)transiently bound to the protein.
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Question
The predominant structural feature in myosin molecules is:

A)a β\beta structure.
B)an α\alpha helix.
C)the Fab domain.
D)the light chain.
E)the meromyosin domain.
Question
An allosteric interaction between a ligand and a protein is one in which:

A)binding of a molecule to a binding site affects binding of additional molecules to the same site.
B)binding of a molecule to a binding site affects binding properties of another site on the protein.
C)binding of the ligand to the protein is covalent.
D)multiple molecules of the same ligand can bind to the same binding site.
E)two different ligands can bind to the same binding site.
Question
The interactions of ligands with proteins:

A)are relatively nonspecific.
B)are relatively rare in biological systems.
C)are usually irreversible.
D)are usually transient.
E)usually result in the inactivation of the proteins.
Question
When oxygen binds to a heme-containing protein,the two open coordination bonds of Fe2+ are occupied by:

A)one O atom and one amino acid atom.
B)one O2 molecule and one amino acid atom.
C)one O2 molecule and one heme atom.
D)two O atoms.
E)two O2 molecules.
Question
In hemoglobin,the transition from T state to R state (low to high affinity)is triggered by:

A)Fe2+ binding.
B)heme binding.
C)oxygen binding.
D)subunit association.
E)subunit dissociation.
Question
Which of the following is not correct concerning 2,3-bisphosphoglycerate (BPG)?

A)It binds at a distance from the heme groups of hemoglobin.
B)It binds with lower affinity to fetal hemoglobin than to adult hemoglobin.
C)It increases the affinity of hemoglobin for oxygen.
D)It is an allosteric modulator.
E)It is normally found associated with the hemoglobin extracted from red blood cells.
Question
Patients with chronic hypoxia (low O2 levels)due to decreased lung function may adapt by increasing their circulating BPG levels.Predict which of the following will be true for such a patient.

A)p50 for O2 will be decreased.
B)p50 for O2 will be increased.
C)The R-state of hemoglobin will be favored.
D)O2 binding to hemoglobin will be hyperbolic.
E)None of the above
Question
The fundamental cause of sickle-cell disease is a change in the structure of:

A)blood.
B)capillaries.
C)hemoglobin.
D)red cells.
E)the heart.
Question
Which of the following generalizations concerning motor proteins is correct?

A)They convert chemical energy into kinetic energy.
B)They convert chemical energy into potential energy.
C)They convert kinetic energy into chemical energy.
D)They convert kinetic energy into rotational energy.
E)They convert potential energy into chemical energy.
Question
Neuroglobin is a member of the globin family found in neurons.It is a monomeric protein that helps protect the brain from hypoxia (low O2).Identify the correct statement(s)about neuroglobin below.
a-It binds O2 with a hyperbolic binding curve.
b-It binds O2 with a sigmoidal binding curve.
c-It binds O2 with higher affinity than hemoglobin.
d-It binds O2 with lower affinity than hemoglobin.

A)a and c
B)a and d
C)b and c
D)b and d
E)None of the above
Question
Which of the following parts of the IgG molecule are not involved in binding to an antigen?

A)Fab
B)Fc
C)Heavy chain
D)Light chain
E)Variable domain
Question
An individual molecular structure within an antigen to which an individual antibody binds is as a(n):

A)antigen.
B)epitope.
C)Fab region.
D)Fc region
E)MHC site.
Question
A monoclonal antibody differs from a polyclonal antibody in that monoclonal antibodies:

A)are labeled with chemicals that can be visualized.
B)are produced by cells from the same organism that produced the antigen.
C)are synthesized by a population of identical,or "cloned," cells.
D)are synthesized only in living organisms.
E)have only a single polypeptide chain that can recognize an antigen.
Question
Which of the following statements about protein-ligand binding is correct?

A)The Ka is equal to the concentration of ligand when all of the binding sites are occupied.
B)The Ka is independent of such conditions as salt concentration and pH.
C)The larger the Ka (association constant),the weaker the affinity.
D)The larger the Ka,the faster is the binding.
E)The larger the Ka,the smaller the Kd (dissociation constant).
Question
In the binding of oxygen to myoglobin,the relationship between the concentration of oxygen and the fraction of binding sites occupied can best be described as:

A)hyperbolic.
B)linear with a negative slope.
C)linear with a positive slope.
D)random.
E)sigmoidal.
Question
The amino acid substitution of Val for Glu in Hemoglobin S results in aggregation of the protein because of ___________ interactions between molecules.

A)covalent
B)disulfide
C)hydrogen bonding
D)hydrophobic
E)ionic
Question
Which of the following is not correct concerning cooperative binding of a ligand to a protein?

A)It is usually a form of allosteric interaction.
B)It is usually associated with proteins with multiple subunits.
C)It rarely occurs in enzymes.
D)It results in a nonlinear Hill Plot.
E)It results in a sigmoidal binding curve.
Question
Carbon monoxide (CO)is toxic to humans because:

A)it binds to myoglobin and causes it to denature.
B)it is rapidly converted to toxic CO2.
C)it binds to the globin portion of hemoglobin and prevents the binding of O2.
D)it binds to the Fe in hemoglobin and prevents the binding of O2.
E)it binds to the heme portion of hemoglobin and causes heme to unbind from hemoglobin.
Question
Myoglobin and the subunits of hemoglobin have:

A)no obvious structural relationship.
B)very different primary and tertiary structures.
C)very similar primary and tertiary structures.
D)very similar primary structures,but different tertiary structures.
E)very similar tertiary structures,but different primary structures.
Question
Describe how you would determine the Ka (association constant)for a ligand and a protein.
Question
(a)What is the effect of pH on the binding of oxygen to hemoglobin (the Bohr Effect)?
(b)Briefly describe the mechanism of this effect.
Question
Describe how immunoaffinity chromatography is performed.
Question
What fraction of ligand binding sites are occupied ( θ\theta )when [ligand] = Kd? Show your work.
Question
During muscle contraction,hydrolysis of ATP results in a change in the:

A)conformation of actin.
B)conformation of myosin.
C)structure of the myofibrils.
D)structure of the sarcoplasmic reticulum.
E)structure of the Z disk.
Question
Explain why most multicellular organisms use an iron-containing protein for oxygen binding rather than free Fe2+.Your answer should include an explanation of (a)the role of heme and (b)the role of the protein itself.
Question
Describe briefly the basic structure of an IgG protein molecule.
Question
Describe briefly the two principal models for the cooperative binding of ligands to proteins with multiple binding sites.
Question
Fetal hemoglobin binds BPG with lower affinity than adult hemoglobin.How does this property facilitate tranfers of O2 from mother to fetus?
Question
Describe the concept of "induced fit" in ligand-protein binding.
Question
Explain why the structure of myoglobin makes it function well as an oxygen-storage protein,whereas the structure of hemoglobin makes it function well as an oxygen-transport protein.
Question
Why is carbon monoxide (CO)toxic to aerobic organisms?
Question
The energy that is released by the hydrolysis of ATP by actin is used for:

A)actin filament assembly.
B)actin filament disassembly.
C)actin-myosin assembly.
D)actin-myosin disassembly.
E)muscle contraction.
Question
What is the concept of "induced fit" as it applies to antigen-antibody binding?
Question
Why is it likely that the immune system can produce a specific antibody that can recognize and bind to any specific chemical structure?
Question
What is the chemical basis for the specificity of binding of an immunoglobin antibody to a particular antigen?
Question
Explain briefly why the relative affinity of heme for oxygen and carbon monoxide is changed by the presence of the myoglobin protein.
Question
How does BPG binding to hemoglobin decrease its affinity for oxygen?
Question
For the binding of a ligand to a protein,what is the relationship between the Ka (association constant),the Kd (dissociation constant),and the affinity of the protein for the ligand?
Question
What properties of antibodies make them useful biochemical reagents? Describe one biochemical application of antibodies (with more than just the name of the technique).
Question
What is the relationship between G-actin and F-actin?
Question
What is the role of ATP and ATP hydrolysis in the cycle of actin-myosin association and disassociation that leads to muscle contraction?
Question
Describe the cycle of actin-myosin association and disassociation that leads to muscle contraction.
Question
Although the myosin molecule "walks" along actin in discrete steps,you are able to make smooth motions using your muscles.Explain how this is possible.
Question
Describe briefly the structure of myosin.
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Deck 5: Protein Function
1
A prosthetic group of a protein is a non-protein structure that is:

A)a ligand of the protein.
B)a part of the secondary structure of the protein.
C)a substrate of the protein.
D)permanently associated with the protein.
E)transiently bound to the protein.
permanently associated with the protein.
2
The predominant structural feature in myosin molecules is:

A)a β\beta structure.
B)an α\alpha helix.
C)the Fab domain.
D)the light chain.
E)the meromyosin domain.
an α\alpha helix.
3
An allosteric interaction between a ligand and a protein is one in which:

A)binding of a molecule to a binding site affects binding of additional molecules to the same site.
B)binding of a molecule to a binding site affects binding properties of another site on the protein.
C)binding of the ligand to the protein is covalent.
D)multiple molecules of the same ligand can bind to the same binding site.
E)two different ligands can bind to the same binding site.
binding of a molecule to a binding site affects binding properties of another site on the protein.
4
The interactions of ligands with proteins:

A)are relatively nonspecific.
B)are relatively rare in biological systems.
C)are usually irreversible.
D)are usually transient.
E)usually result in the inactivation of the proteins.
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5
When oxygen binds to a heme-containing protein,the two open coordination bonds of Fe2+ are occupied by:

A)one O atom and one amino acid atom.
B)one O2 molecule and one amino acid atom.
C)one O2 molecule and one heme atom.
D)two O atoms.
E)two O2 molecules.
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6
In hemoglobin,the transition from T state to R state (low to high affinity)is triggered by:

A)Fe2+ binding.
B)heme binding.
C)oxygen binding.
D)subunit association.
E)subunit dissociation.
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Unlock for access to all 45 flashcards in this deck.
Unlock Deck
k this deck
7
Which of the following is not correct concerning 2,3-bisphosphoglycerate (BPG)?

A)It binds at a distance from the heme groups of hemoglobin.
B)It binds with lower affinity to fetal hemoglobin than to adult hemoglobin.
C)It increases the affinity of hemoglobin for oxygen.
D)It is an allosteric modulator.
E)It is normally found associated with the hemoglobin extracted from red blood cells.
Unlock Deck
Unlock for access to all 45 flashcards in this deck.
Unlock Deck
k this deck
8
Patients with chronic hypoxia (low O2 levels)due to decreased lung function may adapt by increasing their circulating BPG levels.Predict which of the following will be true for such a patient.

A)p50 for O2 will be decreased.
B)p50 for O2 will be increased.
C)The R-state of hemoglobin will be favored.
D)O2 binding to hemoglobin will be hyperbolic.
E)None of the above
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Unlock for access to all 45 flashcards in this deck.
Unlock Deck
k this deck
9
The fundamental cause of sickle-cell disease is a change in the structure of:

A)blood.
B)capillaries.
C)hemoglobin.
D)red cells.
E)the heart.
Unlock Deck
Unlock for access to all 45 flashcards in this deck.
Unlock Deck
k this deck
10
Which of the following generalizations concerning motor proteins is correct?

A)They convert chemical energy into kinetic energy.
B)They convert chemical energy into potential energy.
C)They convert kinetic energy into chemical energy.
D)They convert kinetic energy into rotational energy.
E)They convert potential energy into chemical energy.
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Unlock for access to all 45 flashcards in this deck.
Unlock Deck
k this deck
11
Neuroglobin is a member of the globin family found in neurons.It is a monomeric protein that helps protect the brain from hypoxia (low O2).Identify the correct statement(s)about neuroglobin below.
a-It binds O2 with a hyperbolic binding curve.
b-It binds O2 with a sigmoidal binding curve.
c-It binds O2 with higher affinity than hemoglobin.
d-It binds O2 with lower affinity than hemoglobin.

A)a and c
B)a and d
C)b and c
D)b and d
E)None of the above
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12
Which of the following parts of the IgG molecule are not involved in binding to an antigen?

A)Fab
B)Fc
C)Heavy chain
D)Light chain
E)Variable domain
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k this deck
13
An individual molecular structure within an antigen to which an individual antibody binds is as a(n):

A)antigen.
B)epitope.
C)Fab region.
D)Fc region
E)MHC site.
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Unlock for access to all 45 flashcards in this deck.
Unlock Deck
k this deck
14
A monoclonal antibody differs from a polyclonal antibody in that monoclonal antibodies:

A)are labeled with chemicals that can be visualized.
B)are produced by cells from the same organism that produced the antigen.
C)are synthesized by a population of identical,or "cloned," cells.
D)are synthesized only in living organisms.
E)have only a single polypeptide chain that can recognize an antigen.
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Unlock for access to all 45 flashcards in this deck.
Unlock Deck
k this deck
15
Which of the following statements about protein-ligand binding is correct?

A)The Ka is equal to the concentration of ligand when all of the binding sites are occupied.
B)The Ka is independent of such conditions as salt concentration and pH.
C)The larger the Ka (association constant),the weaker the affinity.
D)The larger the Ka,the faster is the binding.
E)The larger the Ka,the smaller the Kd (dissociation constant).
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k this deck
16
In the binding of oxygen to myoglobin,the relationship between the concentration of oxygen and the fraction of binding sites occupied can best be described as:

A)hyperbolic.
B)linear with a negative slope.
C)linear with a positive slope.
D)random.
E)sigmoidal.
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Unlock for access to all 45 flashcards in this deck.
Unlock Deck
k this deck
17
The amino acid substitution of Val for Glu in Hemoglobin S results in aggregation of the protein because of ___________ interactions between molecules.

A)covalent
B)disulfide
C)hydrogen bonding
D)hydrophobic
E)ionic
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Unlock for access to all 45 flashcards in this deck.
Unlock Deck
k this deck
18
Which of the following is not correct concerning cooperative binding of a ligand to a protein?

A)It is usually a form of allosteric interaction.
B)It is usually associated with proteins with multiple subunits.
C)It rarely occurs in enzymes.
D)It results in a nonlinear Hill Plot.
E)It results in a sigmoidal binding curve.
Unlock Deck
Unlock for access to all 45 flashcards in this deck.
Unlock Deck
k this deck
19
Carbon monoxide (CO)is toxic to humans because:

A)it binds to myoglobin and causes it to denature.
B)it is rapidly converted to toxic CO2.
C)it binds to the globin portion of hemoglobin and prevents the binding of O2.
D)it binds to the Fe in hemoglobin and prevents the binding of O2.
E)it binds to the heme portion of hemoglobin and causes heme to unbind from hemoglobin.
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Unlock Deck
k this deck
20
Myoglobin and the subunits of hemoglobin have:

A)no obvious structural relationship.
B)very different primary and tertiary structures.
C)very similar primary and tertiary structures.
D)very similar primary structures,but different tertiary structures.
E)very similar tertiary structures,but different primary structures.
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k this deck
21
Describe how you would determine the Ka (association constant)for a ligand and a protein.
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22
(a)What is the effect of pH on the binding of oxygen to hemoglobin (the Bohr Effect)?
(b)Briefly describe the mechanism of this effect.
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k this deck
23
Describe how immunoaffinity chromatography is performed.
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24
What fraction of ligand binding sites are occupied ( θ\theta )when [ligand] = Kd? Show your work.
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k this deck
25
During muscle contraction,hydrolysis of ATP results in a change in the:

A)conformation of actin.
B)conformation of myosin.
C)structure of the myofibrils.
D)structure of the sarcoplasmic reticulum.
E)structure of the Z disk.
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Unlock for access to all 45 flashcards in this deck.
Unlock Deck
k this deck
26
Explain why most multicellular organisms use an iron-containing protein for oxygen binding rather than free Fe2+.Your answer should include an explanation of (a)the role of heme and (b)the role of the protein itself.
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k this deck
27
Describe briefly the basic structure of an IgG protein molecule.
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28
Describe briefly the two principal models for the cooperative binding of ligands to proteins with multiple binding sites.
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29
Fetal hemoglobin binds BPG with lower affinity than adult hemoglobin.How does this property facilitate tranfers of O2 from mother to fetus?
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k this deck
30
Describe the concept of "induced fit" in ligand-protein binding.
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31
Explain why the structure of myoglobin makes it function well as an oxygen-storage protein,whereas the structure of hemoglobin makes it function well as an oxygen-transport protein.
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32
Why is carbon monoxide (CO)toxic to aerobic organisms?
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k this deck
33
The energy that is released by the hydrolysis of ATP by actin is used for:

A)actin filament assembly.
B)actin filament disassembly.
C)actin-myosin assembly.
D)actin-myosin disassembly.
E)muscle contraction.
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k this deck
34
What is the concept of "induced fit" as it applies to antigen-antibody binding?
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k this deck
35
Why is it likely that the immune system can produce a specific antibody that can recognize and bind to any specific chemical structure?
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Unlock for access to all 45 flashcards in this deck.
Unlock Deck
k this deck
36
What is the chemical basis for the specificity of binding of an immunoglobin antibody to a particular antigen?
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k this deck
37
Explain briefly why the relative affinity of heme for oxygen and carbon monoxide is changed by the presence of the myoglobin protein.
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k this deck
38
How does BPG binding to hemoglobin decrease its affinity for oxygen?
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39
For the binding of a ligand to a protein,what is the relationship between the Ka (association constant),the Kd (dissociation constant),and the affinity of the protein for the ligand?
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40
What properties of antibodies make them useful biochemical reagents? Describe one biochemical application of antibodies (with more than just the name of the technique).
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Unlock Deck
k this deck
41
What is the relationship between G-actin and F-actin?
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k this deck
42
What is the role of ATP and ATP hydrolysis in the cycle of actin-myosin association and disassociation that leads to muscle contraction?
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43
Describe the cycle of actin-myosin association and disassociation that leads to muscle contraction.
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44
Although the myosin molecule "walks" along actin in discrete steps,you are able to make smooth motions using your muscles.Explain how this is possible.
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45
Describe briefly the structure of myosin.
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