Question 1

Which of the following is not correct concerning cooperative binding of a ligand to a protein?

Accepted Answer

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. 
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 2

Describe the concept of "induced fit" in ligand-protein binding.

Accepted Answer

Induced fit refers to the structural ada

Question 3

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:

Accepted Answer

A) hyperbolic. 
B) linear with a negative slope. 
C) linear with a positive slope. 
D) random. 
E) sigmoidal. 
A) hyperbolic. 
B) linear with a negative slope. 
C) linear with a positive slope. 
D) random. 
E) sigmoidal.

Question 4

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.

Accepted Answer

The hyperbolic binding of oxygen to the

Question 5

Describe briefly the basic structure of an IgG protein molecule.

Accepted Answer

An IgG protein contains two copies of a

Question 6

Carbon monoxide (CO)is toxic to humans because:

Accepted Answer

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. 
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 7

What is the concept of "induced fit" as it applies to antigen-antibody binding?

Accepted Answer

The conformations of the antigen and ant

Question 8

Fetal hemoglobin binds BPG with lower affinity than adult hemoglobin.How does this property facilitate tranfers of O2 from mother to fetus?

Accepted Answer

Lower affinity for BPG means that fetal

Question 9

What is the role of ATP and ATP hydrolysis in the cycle of actin-myosin association and disassociation that leads to muscle contraction?

Accepted Answer

ATP binding to myosin results in a confo

Question 10

Describe how you would determine the Ka (association constant)for a ligand and a protein.

Accepted Answer

An experiment would be carried out in wh

Question 11

The predominant structural feature in myosin molecules is:

Accepted Answer

A) a$\beta$structure. 
B) an$\alpha$ helix. 
C) the Fab domain. 
D) the light chain. 
E) the meromyosin domain. 
A) a$\beta$structure. 
B) an$\alpha$ helix. 
C) the Fab domain. 
D) the light chain. 
E) the meromyosin domain.

Question 12

The interactions of ligands with proteins:

Accepted Answer

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. 
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 13

Myoglobin and the subunits of hemoglobin have:

Accepted Answer

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. 
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 14

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.

Accepted Answer

A given muscle consists of many bundled

Question 15

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

Accepted Answer

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. 
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.

Question 16

Describe how immunoaffinity chromatography is performed.

Accepted Answer

The specific antibody is covalently atta

Question 17

The amino acid substitution of Val for Glu in Hemoglobin S results in aggregation of the protein because of ___________ interactions between molecules.

Accepted Answer

A) covalent 
B) disulfide 
C) hydrogen bonding 
D) hydrophobic 
E) ionic 
A) covalent 
B) disulfide 
C) hydrogen bonding 
D) hydrophobic 
E) ionic

Question 18

An individual molecular structure within an antigen to which an individual antibody binds is as a(n):

Accepted Answer

A) antigen. 
B) epitope. 
C) Fab region. 
D) Fc region 
E) MHC site. 
A) antigen. 
B) epitope. 
C) Fab region. 
D) Fc region 
E) MHC site.

Question 19

In hemoglobin,the transition from T state to R state (low to high affinity)is triggered by:

Accepted Answer

A) Fe2+ binding. 
B) heme binding. 
C) oxygen binding. 
D) subunit association. 
E) subunit dissociation. 
A) Fe2+ binding. 
B) heme binding. 
C) oxygen binding. 
D) subunit association. 
E) subunit dissociation.

Question 20

Why is it likely that the immune system can produce a specific antibody that can recognize and bind to any specific chemical structure?

Accepted Answer

As a result of genetic recombi

Exam 5: Protein Function

Which of the following is not correct concerning cooperative binding of a ligand to a protein?

Describe the concept of "induced fit" in ligand-protein binding.

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:

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.

Describe briefly the basic structure of an IgG protein molecule.

Carbon monoxide (CO)is toxic to humans because:

What is the concept of "induced fit" as it applies to antigen-antibody binding?

Fetal hemoglobin binds BPG with lower affinity than adult hemoglobin.How does this property facilitate tranfers of O2 from mother to fetus?

What is the role of ATP and ATP hydrolysis in the cycle of actin-myosin association and disassociation that leads to muscle contraction?

Describe how you would determine the Ka (association constant)for a ligand and a protein.

The predominant structural feature in myosin molecules is:

The interactions of ligands with proteins:

Myoglobin and the subunits of hemoglobin have:

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.

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

Describe how immunoaffinity chromatography is performed.

The amino acid substitution of Val for Glu in Hemoglobin S results in aggregation of the protein because of ___________ interactions between molecules.

An individual molecular structure within an antigen to which an individual antibody binds is as a(n):

In hemoglobin,the transition from T state to R state (low to high affinity)is triggered by:

Why is it likely that the immune system can produce a specific antibody that can recognize and bind to any specific chemical structure?

The Foundations of Biochemistry

Water

Amino Acids, peptides, and Proteins

The Three-Dimensional Structure of Proteins

Enzymes

Carbohydrates and Glycobiology

Nucleotides and Nucleic Acids

Recombinant Dna Technology

Lipids

Biological Membranes and Transport

Biosignaling

Principles of Bioenergetics

Glycolysis, gluconeogenesis, and the Pentose Phosphate Pathway

Principles of Metabolic Regulation

The Citric Acid Cycle

Fatty Acid Catabolism

Amino Acid Oxidation and the Production of Urea

Oxidative Phosphorylation and Photophosphorylation

Carbohydrate Biosynthesis in Plants and Bacteria

Lipid Biosynthesis

Biosynthesis of Amino Acids, nucleotides, and Related Molecules

Integration and Hormonal Regulation of Mammalian Metabolism

Genes and Chromosomes

Dna Metabolism

Rna Metabolism

Protein Metabolism

Regulation of Gene Expression

Filters

Fetal hemoglobin binds BPG with lower affinity than adult hemoglobin.How does this property facilitate tranfers of O₂ from mother to fetus?

Describe how you would determine the K_a (association constant)for a ligand and a protein.