Question 1

Disulfide bonds are most important in this type of structure:

Accepted Answer

A)  primary structure 
B)  secondary structure 
C)  tertiary structure 
D)  quaternary structure 
E)  All of these 
A)  primary structure 
B)  secondary structure 
C)  tertiary structure 
D)  quaternary structure 
E)  All of these

Question 2

Generally speaking, this type of protein is water-soluble:

Accepted Answer

A)  Fibrous. 
B)  Globular. 
C)  Both fibrous and globular proteins are usually water-soluble. 
D)  Neither fibrous nor globular proteins are usually water-soluble. 
E)  You cannot generalize about the solubility of fibrous or globular proteins. 
A)  Fibrous. 
B)  Globular. 
C)  Both fibrous and globular proteins are usually water-soluble. 
D)  Neither fibrous nor globular proteins are usually water-soluble. 
E)  You cannot generalize about the solubility of fibrous or globular proteins.

Question 3

Which of the following amino acids is unlikely to be found in an α -helix?

Accepted Answer

A)  phenylalanine 
B)  tryptophan 
C)  proline 
D)  lysine 
A)  phenylalanine 
B)  tryptophan 
C)  proline 
D)  lysine

Question 4

_____ are spherical aggregates of lipids arranged so that the polar head groups are in contact with water and the nonpolar tails are sequestered from water.

Accepted Answer

A)  Liposomes 
B)  Azotosomes 
C)  Escheriosomes 
D)  Chromosomes 
A)  Liposomes 
B)  Azotosomes 
C)  Escheriosomes 
D)  Chromosomes

Question 5

Exhibit 4B   Refer to Exhibit 4B. The type of bonding labeled "O" in these figure is:

Accepted Answer

A)  Hydrogen bonding of the peptide backbone 
B)  Covalent bonding involving the R-groups 
C)  Hydrophobic interactions 
D)  Metal ion coordination 
E)  Electrostatic attraction 
A)  Hydrogen bonding of the peptide backbone 
B)  Covalent bonding involving the R-groups 
C)  Hydrophobic interactions 
D)  Metal ion coordination 
E)  Electrostatic attraction

Question 6

Which of the following factors tend to destabilize α -helices?

Accepted Answer

A)  clusters of amino acids with bulky R-groups 
B)  clusters of amino acids with similarly charged R-groups 
C)  Both of these. 
D)  Neither of these 
A)  clusters of amino acids with bulky R-groups 
B)  clusters of amino acids with similarly charged R-groups 
C)  Both of these. 
D)  Neither of these

Question 7

Which of the following best describes what happens when hemoglobin binds bis phosphoglyceric acid (BPG)?

Accepted Answer

A)  Binding of BPG leads to tighter binding of oxygen. 
B)  Binding of BPG allows maternal (adult) Hb to bind oxygen more tightly than fetal Hb. 
C)  Binding of BPG is important to the allosteric nature of hemoglobin 
D)  Binding of BPG causes the subunits of hemoglobin to separate. 
A)  Binding of BPG leads to tighter binding of oxygen. 
B)  Binding of BPG allows maternal (adult) Hb to bind oxygen more tightly than fetal Hb. 
C)  Binding of BPG is important to the allosteric nature of hemoglobin 
D)  Binding of BPG causes the subunits of hemoglobin to separate.

Question 8

Which of the following is often found connecting the strands of an antiparallel β -sheet?

Accepted Answer

A)  β -bulge 
B)  reverse turn 
C)  α -helix 
D)  prosthetic group 
A)  β -bulge 
B)  reverse turn 
C)  α -helix 
D)  prosthetic group

Question 9

The binding of oxygen to hemoglobin differs from the oxygen-binding behavior of myoglobin because

Accepted Answer

A)  oxygen binding to hemoglobin is cooperative. 
B)  oxygen binding to myoglobin is cooperative. 
C)  hemoglobin is not an allosteric protein. 
D)  the oxygen-binding curve of hemoglobin is hyperbolic. 
A)  oxygen binding to hemoglobin is cooperative. 
B)  oxygen binding to myoglobin is cooperative. 
C)  hemoglobin is not an allosteric protein. 
D)  the oxygen-binding curve of hemoglobin is hyperbolic.

Question 10

Exhibit 4B   Refer to Exhibit 4B. Which one shows hydrogen bonding of the peptide backbone?

Accepted Answer

A)  M 
B)  N 
C)  P 
D)  M and N 
E)  All of these 
A)  M 
B)  N 
C)  P 
D)  M and N 
E)  All of these

Question 11

Which of the following forces are involved in maintaining the primary structure of a protein?

Accepted Answer

A)  covalent bonds 
B)  hydrogen bonds 
C)  ionic interactions 
D)  hydrophobic interactions 
A)  covalent bonds 
B)  hydrogen bonds 
C)  ionic interactions 
D)  hydrophobic interactions

Question 12

Assuming the oligopeptide ALPHAHELICKS forms one continuous α -helix, the carbonyl oxygen of the glutamic acid residue is hydrogen bonded to the amide nitrogen of

Accepted Answer

A)  leucine. 
B)  isoleucine. 
C)  cysteine. 
D)  lysine. 
E)  serine. 
A)  leucine. 
B)  isoleucine. 
C)  cysteine. 
D)  lysine. 
E)  serine.

Question 13

Which of the following diseases is based on abnormal protein folding?

Accepted Answer

A)  Alzheimers disease 
B)  Mad Cow Disease 
C)  Prion diseases 
D)  Frontotemporal dementia 
E)  All of the choices 
A)  Alzheimers disease 
B)  Mad Cow Disease 
C)  Prion diseases 
D)  Frontotemporal dementia 
E)  All of the choices

Question 14

What happens when a protein is denatured?

Accepted Answer

A)  Its secondary structure is disrupted but its primary structure remains intact. 
B)  Its primary structure is disrupted but its secondary structure remains intact. 
C)  It is broken apart into its constituent amino acids. 
D)  It becomes all α -helix. 
A)  Its secondary structure is disrupted but its primary structure remains intact. 
B)  Its primary structure is disrupted but its secondary structure remains intact. 
C)  It is broken apart into its constituent amino acids. 
D)  It becomes all α -helix.

Question 15

Which of the following can result in protein denaturation?

Accepted Answer

A)  heat 
B)  extremes of pH 
C)  detergents 
D)  all of the above 
A)  heat 
B)  extremes of pH 
C)  detergents 
D)  all of the above

Question 16

Fibrous proteins

Accepted Answer

A)  are always composed of helical structures. 
B)  are always composed of β -sheets. 
C)  can be composed of either helical or β -sheet structures. 
D)  are always water soluble 
A)  are always composed of helical structures. 
B)  are always composed of β -sheets. 
C)  can be composed of either helical or β -sheet structures. 
D)  are always water soluble

Question 17

Variations in the structure of hemoglobin

Accepted Answer

A)  do not always have an adverse effect on health 
B)  can alter the binding of heme to the protein 
C)  can occur on the surface of the protein 
D)  all of these 
A)  do not always have an adverse effect on health 
B)  can alter the binding of heme to the protein 
C)  can occur on the surface of the protein 
D)  all of these

Question 18

Proteins that aid in the correct and timely folding of other proteins are called

Accepted Answer

A)  motifs. 
B)  chaperones. 
C)  liposomes. 
D)  cooperative. 
A)  motifs. 
B)  chaperones. 
C)  liposomes. 
D)  cooperative.

Question 19

Which of the following forces are involved in maintaining the quaternary structure of a protein?

Accepted Answer

A)  hydrogen bonds 
B)  ionic interactions 
C)  hydrophobic interactions 
D)  All of these 
A)  hydrogen bonds 
B)  ionic interactions 
C)  hydrophobic interactions 
D)  All of these

Question 20

Which of the following is the most common function for fibrous proteins?

Accepted Answer

A)  enzymes 
B)  structural roles. 
C)  carrier molecules. 
D)  enzymes and carrier molecules. 
E)  All of these. 
A)  enzymes 
B)  structural roles. 
C)  carrier molecules. 
D)  enzymes and carrier molecules. 
E)  All of these.

Exam 4: The Three Dimensional Structure of Proteins

Disulfide bonds are most important in this type of structure:

Generally speaking, this type of protein is water-soluble:

Which of the following amino acids is unlikely to be found in an α -helix?

_____ are spherical aggregates of lipids arranged so that the polar head groups are in contact with water and the nonpolar tails are sequestered from water.

Exhibit 4B Refer to Exhibit 4B. The type of bonding labeled "O" in these figure is:

Which of the following factors tend to destabilize α -helices?

Which of the following best describes what happens when hemoglobin binds bis phosphoglyceric acid (BPG)?

Which of the following is often found connecting the strands of an antiparallel β -sheet?

The binding of oxygen to hemoglobin differs from the oxygen-binding behavior of myoglobin because

Exhibit 4B Refer to Exhibit 4B. Which one shows hydrogen bonding of the peptide backbone?

Which of the following forces are involved in maintaining the primary structure of a protein?

Assuming the oligopeptide ALPHAHELICKS forms one continuous α -helix, the carbonyl oxygen of the glutamic acid residue is hydrogen bonded to the amide nitrogen of

Which of the following diseases is based on abnormal protein folding?

What happens when a protein is denatured?

Which of the following can result in protein denaturation?

Fibrous proteins

Variations in the structure of hemoglobin

Proteins that aid in the correct and timely folding of other proteins are called

Which of the following forces are involved in maintaining the quaternary structure of a protein?

Which of the following is the most common function for fibrous proteins?

Biochemistry and the Organization of Cells

Water the Solvent for Biochemical Reactions

Amino Acids and Peptides

Protein Purification and Characterization Techniques

The Behavior of Proteins Enzymes

The Behavior of Proteins Enzymes Mechanisms and Control

Lipids and Proteins Are Associated in Biological Membranes

Nucleic Acids How Structure Conveys Information

Biosynthesis of Nucleic Acids Replication

Transcription of the Genetic Code the Biosynthesis of Rna

Protein Synthesis Translation of the Genetic Message

Nucleic Acid Biotechnology Techniques

Viruses Cancer and Immunology

The Importance of Energy Changes and Electron Transfer in Metabolism

Carbohydrates

Glycolysis

Storage Mechanisms and Control in Carbohydrate Metabolism

The Citric Acid Cycle

Electron Transport and Oxidative Phosphorylation

Lipid Metabolism

Photosynthesis

The Metabolism of Nitrogen

Integration of Metabolism Cellular Signaling

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