Question 1

The information needed for the structure of a protein is contained in

Accepted Answer

A)  amino acid composition 
B)  primary structure 
C)  secondary structure 
D)  tertiary structure 
A)  amino acid composition 
B)  primary structure 
C)  secondary structure 
D)  tertiary structure B

Question 2

In allosteric interactions

Accepted Answer

A)  proteins that consist of a single polypeptide chain form aggregates. 
B)  disulfide bonds are broken. 
C)  changes that take place in one site of a protein cause changes at a distant site. 
D)  metal ions always bind to the protein. 
A)  proteins that consist of a single polypeptide chain form aggregates. 
B)  disulfide bonds are broken. 
C)  changes that take place in one site of a protein cause changes at a distant site. 
D)  metal ions always bind to the protein. C

Question 3

Exhibit 4B
  
-Refer to Exhibit 4B. Which one shows hydrogen bonding of R-groups?

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 C

Question 4

The tertiary structure of a protein is usually a result of which of the following interactions?

Accepted Answer

A)  intramolecular hydrogen bonding 
B)  electrostatic interactions 
C)  hydrophobic interactions 
D)  all of these 
A)  intramolecular hydrogen bonding 
B)  electrostatic interactions 
C)  hydrophobic interactions 
D)  all of these

Question 5

Which of the following proteins is not homologous with the others?

Accepted Answer

A)  myoglogin 
B)  α-chain of hemoglobin 
C)  β-chain of hemoglobin 
D)  collagen 
A)  myoglogin 
B)  α-chain of hemoglobin 
C)  β-chain of hemoglobin 
D)  collagen

Question 6

Why does myoglobin have a histidine that prevents both O2 and CO from binding perpendicularly to the heme plane?

Accepted Answer

A)  This increases myoglobin's affinity for O2. 
B)  This increases myoglobin's affinity for CO. 
C)  This lessens the difference in myoglobin's affinity for CO versus O2. 
D)  This prevents the iron of the heme from being oxidized. 
A)  This increases myoglobin's affinity for O2. 
B)  This increases myoglobin's affinity for CO. 
C)  This lessens the difference in myoglobin's affinity for CO versus O2. 
D)  This prevents the iron of the heme from being oxidized.

Question 7

Which of the following amino acid residues would most likely be found in the interior of a globular protein?

Accepted Answer

A)  glutamic acid 
B)  lysine 
C)  leucine 
D)  serine 
A)  glutamic acid 
B)  lysine 
C)  leucine 
D)  serine

Question 8

The sequence of monomers in any polymer is 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 9

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.

Question 10

Refer to Exhibit 4A. The carboxyl terminal end is:

Accepted Answer

A)  Arg 
B)  Cys 
C)  Gln 
D)  Met 
E)  None of these. 
A)  Arg 
B)  Cys 
C)  Gln 
D)  Met 
E)  None of these.

Question 11

Vitamin C (ascorbic acid) prevents scurvy because

Accepted Answer

A)  it is involved in the formation of the proper β-sheet structure of collagen. 
B)  it is involved in the metabolism of heme used in hemoglobin. 
C)  it encourages the formation of disulfide linkages in collagen. 
D)  it is an unusual amino acid found in the primary structure of collagen. 
E)  it is used to hydroxylate prolines in the primary structure of collagen. 
A)  it is involved in the formation of the proper β-sheet structure of collagen. 
B)  it is involved in the metabolism of heme used in hemoglobin. 
C)  it encourages the formation of disulfide linkages in collagen. 
D)  it is an unusual amino acid found in the primary structure of collagen. 
E)  it is used to hydroxylate prolines in the primary structure of collagen.

Question 12

Exhibit 4B
  
-Refer to Exhibit 4B. Which one shows covalent bonding of R-groups?

Accepted Answer

A)  K 
B)  L 
C)  O 
D)  K and L 
E)  All of these 
A)  K 
B)  L 
C)  O 
D)  K and L 
E)  All of these

Question 13

Hydrophobic interactions may occur between the R groups of which of the following amino acids?

Accepted Answer

A)  tyrosine and glycine 
B)  arginine and histidine 
C)  phenylalanine and tryptophan 
D)  valine and asparagine 
A)  tyrosine and glycine 
B)  arginine and histidine 
C)  phenylalanine and tryptophan 
D)  valine and asparagine

Question 14

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 15

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

Accepted Answer

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

Question 16

The overall folding of a single protein subunit is called:

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 17

Exhibit 4B
  
-Refer to Exhibit 4B. Which one shows electrostatic attraction of R-groups?

Accepted Answer

A)  K 
B)  L 
C)  O 
D)  K and L 
E)  All of these 
A)  K 
B)  L 
C)  O 
D)  K and L 
E)  All of these

Question 18

The oxygen binding curve of which of the following is the closest to that of myoglobin?

Accepted Answer

A)  hemoglobin at pH 6.8 
B)  hemoglobin that lacks BPG 
C)  maternal hemoglobin 
D)  fetal hemoglobin 
A)  hemoglobin at pH 6.8 
B)  hemoglobin that lacks BPG 
C)  maternal hemoglobin 
D)  fetal hemoglobin

Question 19

What would happen to hemoglobin if the BPG were removed?

Accepted Answer

A)  It would not bind oxygen 
B)  It would dissociate into monomers 
C)  its oxygen binding curve would resemble that of myoglobin 
D)  all of the choices 
A)  It would not bind oxygen 
B)  It would dissociate into monomers 
C)  its oxygen binding curve would resemble that of myoglobin 
D)  all of the choices

Question 20

In sickle-cell anemia hemoglobin

Accepted Answer

A)  the four subunits of hemoglobin dissociate from one another 
B)  the heme group is lost from all subunits 
C)  the iron is in the Fe(III) form rather than the normal Fe(II) 
D)  groups of hemoglobin molecules aggregate with each other 
A)  the four subunits of hemoglobin dissociate from one another 
B)  the heme group is lost from all subunits 
C)  the iron is in the Fe(III) form rather than the normal Fe(II) 
D)  groups of hemoglobin molecules aggregate with each other

Exam 4: The Three-Dimensional Structure of Proteins

The information needed for the structure of a protein is contained in

In allosteric interactions

Exhibit 4B -Refer to Exhibit 4B. Which one shows hydrogen bonding of R-groups?

The tertiary structure of a protein is usually a result of which of the following interactions?

Which of the following proteins is not homologous with the others?

Why does myoglobin have a histidine that prevents both O2 and CO from binding perpendicularly to the heme plane?

Which of the following amino acid residues would most likely be found in the interior of a globular protein?

The sequence of monomers in any polymer is this type of structure:

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

Refer to Exhibit 4A. The carboxyl terminal end is:

Vitamin C (ascorbic acid) prevents scurvy because

Exhibit 4B -Refer to Exhibit 4B. Which one shows covalent bonding of R-groups?

Hydrophobic interactions may occur between the R groups of which of the following amino acids?

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

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

The overall folding of a single protein subunit is called:

Exhibit 4B -Refer to Exhibit 4B. Which one shows electrostatic attraction of R-groups?

The oxygen binding curve of which of the following is the closest to that of myoglobin?

What would happen to hemoglobin if the BPG were removed?

In sickle-cell anemia hemoglobin

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: 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

Filters

Why does myoglobin have a histidine that prevents both O₂ and CO from binding perpendicularly to the heme plane?