Question 1

In the b-pleated sheet conformation

Accepted Answer

A)  there are hydrogen bonds perpendicular to the direction of the polypeptide chain. 
B)  the polypeptide chain is almost fully extended. 
C)  the polypeptide chains may be hydrogen bonded together in a parallel or antiparallel orientation. 
D)  all of these 
A)  there are hydrogen bonds perpendicular to the direction of the polypeptide chain. 
B)  the polypeptide chain is almost fully extended. 
C)  the polypeptide chains may be hydrogen bonded together in a parallel or antiparallel orientation. 
D)  all of these

Question 2

Heme would best be described as a

Accepted Answer

A)  motif. 
B)  domain. 
C)  prosthetic group. 
D)  helix. 
A)  motif. 
B)  domain. 
C)  prosthetic group. 
D)  helix.

Question 3

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 4

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

Question 5

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 6

In the a-helix

Accepted Answer

A)  there are no hydrogen bonds 
B)  the peptide chain is fully extended 
C)  the peptide chain bends back on itself 
D)  there are hydrogen bonds parallel to the helix axis 
A)  there are no hydrogen bonds 
B)  the peptide chain is fully extended 
C)  the peptide chain bends back on itself 
D)  there are hydrogen bonds parallel to the helix axis

Question 7

In the Bohr effect the binding of oxygen to hemoglobin

Accepted Answer

A)  is increased by the presence of Na+ 
B)  is increased by the presence of H+ and CO2 
C)  is decreased by the presence of H+ and CO2 
D)  is unchanged 
A)  is increased by the presence of Na+ 
B)  is increased by the presence of H+ and CO2 
C)  is decreased by the presence of H+ and CO2 
D)  is unchanged

Question 8

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 9

Assuming the oligopeptide ALPHAHELICKS forms one continuous a-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 10

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 11

Vitamin C (ascorbic acid) prevents scurvy because

Accepted Answer

A)  it is involved in the formation of the proper b-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 b-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

What is the major force that drives nonpolar substances out of aqueous solution?

Accepted Answer

A)  Increased enthalpy of hydrophobic bonds formed between solute molecules. 
B)  Decreased entropy of newly organized solute molecules. 
C)  Increased entropy of newly organized solute molecules. 
D)  Increased enthalpy of H-bonds in the solvent water. 
E)  Increased entropy of solvent water molecules. 
A)  Increased enthalpy of hydrophobic bonds formed between solute molecules. 
B)  Decreased entropy of newly organized solute molecules. 
C)  Increased entropy of newly organized solute molecules. 
D)  Increased enthalpy of H-bonds in the solvent water. 
E)  Increased entropy of solvent water molecules.

Question 13

As an animal ages,the amount of cross-linking of collagen in tissue

Accepted Answer

A)  tends to decrease. 
B)  tends to increase. 
C)  tends to remain unchanged. 
A)  tends to decrease. 
B)  tends to increase. 
C)  tends to remain unchanged.

Question 14

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

Question 15

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 16

Which of the following factors tend to destabilize a-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 17

The location of prosthetic groups is shown in this level 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 18

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 19

Which of the following best describes the structure of collagen?

Accepted Answer

A)  It is composed of a single a-helix. 
B)  It is a double helix. 
C)  It is a triple helix 
D)  It is composed primarily of b-sheet. 
A)  It is composed of a single a-helix. 
B)  It is a double helix. 
C)  It is a triple helix 
D)  It is composed primarily of b-sheet.

Question 20

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 a-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 a-helix.

Exam 4: The Three-Dimensional Structure of Proteins

In the b-pleated sheet conformation

Heme would best be described as a

Variations in the structure of hemoglobin

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

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

In the a-helix

In the Bohr effect the binding of oxygen to hemoglobin

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

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

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

Vitamin C (ascorbic acid) prevents scurvy because

What is the major force that drives nonpolar substances out of aqueous solution?

As an animal ages,the amount of cross-linking of collagen in tissue

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

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

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

The location of prosthetic groups is shown in this level of structure:

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

Which of the following best describes the structure of collagen?

What happens when a protein is denatured?

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

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