Question 1

Match each level of organization with a description. A) Overall shape of a protein
B) Repeated pattern of folding
C) Multiple subunits are present
D) Specific order of amino acids
-Primary structure

Accepted Answer

The answer of Match each level of organization with a...

Question 2

Myoglobin has a greater affinity for oxygen than hemoglobin.

Accepted Answer

Myoglobin is a protein found in muscle tissue that plays a role in storing oxygen. It has a higher affinity for oxygen than hemoglobin, the protein found in red blood cells that transports oxygen throughout the body.

Question 3

Ascorbic acid is necessary for the formation of hydroxyproline and hydroxylysine residues before they are incorporated into the collagen protein molecule.

Accepted Answer

The answer of Ascorbic acid is necessary for the formation...

Question 4

For each term select the description that best describes its contribution to the structure of collagen. A) Has $ \mathrm{H} $ bonds which help stabilize the protein
B) Makes the protein rigid
C) Required for hydroxylation
D) Forms covalent cross links
E) Allows tightly wound helix formation
-Glycine

Accepted Answer

The answer of For each term select the description that...

Question 5

For each term select the description that best describes its contribution to the structure of collagen. A) Has $ \mathrm{H} $ bonds which help stabilize the protein
B) Makes the protein rigid
C) Required for hydroxylation
D) Forms covalent cross links
E) Allows tightly wound helix formation
-Proline

Accepted Answer

The answer of For each term select the description that...

Question 6

Match each level of organization with a description. A) Overall shape of a protein
B) Repeated pattern of folding
C) Multiple subunits are present
D) Specific order of amino acids
-Quaternary structure

Accepted Answer

The answer of Match each level of organization with a...

Question 7

Match each level of organization with a description. A) Overall shape of a protein
B) Repeated pattern of folding
C) Multiple subunits are present
D) Specific order of amino acids
-Secondary structure

Accepted Answer

The answer of Match each level of organization with a...

Question 8

The porphyrin prosthetic group is held into the interior of globin molecules by covalent bonds to specific amino acid residues.

Accepted Answer

The porphyrin prosthetic group is not held by covalent bonds, but rather by noncovalent interactions such as hydrophobic and electrostatic interactions.

Question 9

For each term select the description that best describes its contribution to the structure of collagen. A) Has $ \mathrm{H} $ bonds which help stabilize the protein
B) Makes the protein rigid
C) Required for hydroxylation
D) Forms covalent cross links
E) Allows tightly wound helix formation
-Allysine

Accepted Answer

The answer of For each term select the description that...

Question 10

Match the protein organization most associated with the terms) listed below: A) Tertiary
B) Secondary
C) Primary
D) Quaternary
-Cystine

Accepted Answer

Cystine crystals are hexagonal in shape.

Question 11

For each term select the description that best describes its contribution to the structure of collagen. A) Has $ \mathrm{H} $ bonds which help stabilize the protein
B) Makes the protein rigid
C) Required for hydroxylation
D) Forms covalent cross links
E) Allows tightly wound helix formation
-Vitamin C

Accepted Answer

Vitamin C deficiency leads to scurvy, which is characterized by symptoms such as bleeding gums, weakness, and bruising due to its role in collagen synthesis.

Question 12

Match each level of organization with a description. A) Overall shape of a protein
B) Repeated pattern of folding
C) Multiple subunits are present
D) Specific order of amino acids
-Tertiary structure

Accepted Answer

The answer of Match each level of organization with a...

Question 13

Match the protein organization most associated with the terms) listed below: A) Tertiary
B) Secondary
C) Primary
D) Quaternary
-Subunits

Accepted Answer

The answer of Match the protein organization most associated with...

Question 14

Match the protein organization most associated with the terms) listed below: A) Tertiary
B) Secondary
C) Primary
D) Quaternary
-Peptide bonds

Accepted Answer

The answer of Match the protein organization most associated with...

Question 15

Match the protein organization most associated with the terms) listed below: A) Tertiary
B) Secondary
C) Primary
D) Quaternary
-Hydrogen bonds between carbonyl and amino groups

Accepted Answer

The answer of Match the protein organization most associated with...

Question 16

The Bohr effect describes the effect of pH on hemoglobinʹs ability to bind oxygen. Oxygen binds more tightly at low pH and less tightly at higher pH values.

Accepted Answer

The Bohr effect actually describes the opposite: oxygen binds more tightly to hemoglobin at higher pH values and less tightly at lower pH values. This is because a decrease in pH (which corresponds to an increase in hydrogen ion concentration) weakens hemoglobin's affinity for oxygen, facilitating oxygen release to tissues.

Question 17

The hydrophobic crevice of globin prevents complete electron transfer to the oxygen so that the electron returns to the iron atom when oxygen dissociates.

Accepted Answer

This is true because the hydrophobic crevice in globin hinders the access of water molecules and other polar molecules, preventing them from interacting with the oxygen-binding site. This prevents complete electron transfer to the oxygen, allowing the electron to return to the iron atom when oxygen dissociates, instead of being donated to water and forming harmful reactive oxygen species.

Question 18

Cooperative binding and allosterism of hemoglobin allow oxygen to be unloaded at low partial pressures of oxygen in the tissues.

Accepted Answer

Hemoglobin exhibits cooperative binding, meaning that binding of oxygen to one heme group enhances the oxygen-binding affinity of the other heme groups in the tetramer. Allosterism allows for conformational changes in the hemoglobin protein that facilitate the release of oxygen at low partial pressures of oxygen in the tissues.

Question 19

Part of immunoglobulin molecules can be changed in order to bind to a variety of antigens while the amino acid sequence of another part does not change.

Accepted Answer

This is known as the variable region of the immunoglobulin molecule. The constant region, which is responsible for other functions of the molecule, remains unchanged.

Question 20

At high carbon dioxide concentrations the carbamates of hemoglobin can be formed. The carbamates of oxyhemoglobin are less stable than those of deoxyhemoglobin.

Accepted Answer

This is true because at high carbon dioxide concentrations, some of the carbon dioxide can react with water to form bicarbonate ions, which can then react with amino groups on hemoglobin to form carbamates. The formation of these carbamates is favored on deoxyhemoglobin because they bind to different sites than oxygen, whereas oxyhemoglobin already has an oxygen bound to these sites, making carbamate formation less stable.

Quiz 4: Proteins: Three-Dimensional Structure and Function

Match each level of organization with a description. A) Overall shape of a protein B) Repeated pattern of folding C) Multiple subunits are present D) Specific order of amino acids -Primary structure

Myoglobin has a greater affinity for oxygen than hemoglobin.

Ascorbic acid is necessary for the formation of hydroxyproline and hydroxylysine residues before they are incorporated into the collagen protein molecule.

For each term select the description that best describes its contribution to the structure of collagen. A) Has $\mathrm{H}$ bonds which help stabilize the protein B) Makes the protein rigid C) Required for hydroxylation D) Forms covalent cross links E) Allows tightly wound helix formation -Glycine

For each term select the description that best describes its contribution to the structure of collagen. A) Has $\mathrm{H}$ bonds which help stabilize the protein B) Makes the protein rigid C) Required for hydroxylation D) Forms covalent cross links E) Allows tightly wound helix formation -Proline

Match each level of organization with a description. A) Overall shape of a protein B) Repeated pattern of folding C) Multiple subunits are present D) Specific order of amino acids -Quaternary structure

Match each level of organization with a description. A) Overall shape of a protein B) Repeated pattern of folding C) Multiple subunits are present D) Specific order of amino acids -Secondary structure

The porphyrin prosthetic group is held into the interior of globin molecules by covalent bonds to specific amino acid residues.

For each term select the description that best describes its contribution to the structure of collagen. A) Has $\mathrm{H}$ bonds which help stabilize the protein B) Makes the protein rigid C) Required for hydroxylation D) Forms covalent cross links E) Allows tightly wound helix formation -Allysine

Match the protein organization most associated with the terms) listed below: A) Tertiary B) Secondary C) Primary D) Quaternary -Cystine

For each term select the description that best describes its contribution to the structure of collagen. A) Has $\mathrm{H}$ bonds which help stabilize the protein B) Makes the protein rigid C) Required for hydroxylation D) Forms covalent cross links E) Allows tightly wound helix formation -Vitamin C

Match each level of organization with a description. A) Overall shape of a protein B) Repeated pattern of folding C) Multiple subunits are present D) Specific order of amino acids -Tertiary structure

Match the protein organization most associated with the terms) listed below: A) Tertiary B) Secondary C) Primary D) Quaternary -Subunits

Match the protein organization most associated with the terms) listed below: A) Tertiary B) Secondary C) Primary D) Quaternary -Peptide bonds

Match the protein organization most associated with the terms) listed below: A) Tertiary B) Secondary C) Primary D) Quaternary -Hydrogen bonds between carbonyl and amino groups

The Bohr effect describes the effect of pH on hemoglobinʹs ability to bind oxygen. Oxygen binds more tightly at low pH and less tightly at higher pH values.

The hydrophobic crevice of globin prevents complete electron transfer to the oxygen so that the electron returns to the iron atom when oxygen dissociates.

Cooperative binding and allosterism of hemoglobin allow oxygen to be unloaded at low partial pressures of oxygen in the tissues.

Part of immunoglobulin molecules can be changed in order to bind to a variety of antigens while the amino acid sequence of another part does not change.

At high carbon dioxide concentrations the carbamates of hemoglobin can be formed. The carbamates of oxyhemoglobin are less stable than those of deoxyhemoglobin.