Question 1

Noncovalent bonds essential for the formation of the α helix and b-pleated sheet are:

Accepted Answer

A) Disulfide bonds. 
B) Van der Waals interactions. 
C) Salt bridges. 
D) Hydrogen bonds. 
E) Hydrophobic forces. 
A) Disulfide bonds. 
B) Van der Waals interactions. 
C) Salt bridges. 
D) Hydrogen bonds. 
E) Hydrophobic forces. D

Question 2

Histones are proteins that bind to negatively charged phosphate groups of DNA.An amino acid in the histones that can mediate this binding is:

Accepted Answer

A) Valine. 
B) Lysine. 
C) Aspartate. 
D) Cysteine. 
E) Glutamic acid. 
A) Valine. 
B) Lysine. 
C) Aspartate. 
D) Cysteine. 
E) Glutamic acid. B

Question 3

Amino acids at the isoelectric point in the titration curve have a net charge of:

Accepted Answer

A) 1. 
B) +1. 
C) +2. 
D) 0. 
E) -2. 
A) 1. 
B) +1. 
C) +2. 
D) 0. 
E) -2. D

Question 4

Which of the following statements is correct for protein structure?

Accepted Answer

A) The a helix is stabilized primarily by ionic interactions between the side chains of amino acids. 
B) Disulfide bonds are common in cytoplasmic proteins but are not present in most proteins of the extracellular matrix. 
C) The stability of the quaternary structure in proteins is a result of covalent bonds between the subunits. 
D) The heat denaturation of proteins is in most cases reversible by slow cooling. 
E) Glycine and proline do not usually participate in a-helical structures. 
A) The a helix is stabilized primarily by ionic interactions between the side chains of amino acids. 
B) Disulfide bonds are common in cytoplasmic proteins but are not present in most proteins of the extracellular matrix. 
C) The stability of the quaternary structure in proteins is a result of covalent bonds between the subunits. 
D) The heat denaturation of proteins is in most cases reversible by slow cooling. 
E) Glycine and proline do not usually participate in a-helical structures.

Question 5

All naturally occurring amino acids:

Accepted Answer

A) Have more than one α-carbon atom. 
B) Are uncharged at a pH of 7. 
C) Can only have two pKs. 
D) Are chiral, except glycine. 
E) Occur in nature mainly or exclusively in the optically active D-form. 
A) Have more than one α-carbon atom. 
B) Are uncharged at a pH of 7. 
C) Can only have two pKs. 
D) Are chiral, except glycine. 
E) Occur in nature mainly or exclusively in the optically active D-form.

Question 6

The secondary structure of proteins:

Accepted Answer

A) Is maintained by hydrogen bonds. 
B) Is present only in proteins consisting of two or more subunits held together by noncovalent forces. 
C) Refers to any hydrogen-bonded interaction found in proteins. 
D) Implies the presence of a nonprotein moiety bound to the polypeptide. 
E) Is found only in fibrous proteins. 
A) Is maintained by hydrogen bonds. 
B) Is present only in proteins consisting of two or more subunits held together by noncovalent forces. 
C) Refers to any hydrogen-bonded interaction found in proteins. 
D) Implies the presence of a nonprotein moiety bound to the polypeptide. 
E) Is found only in fibrous proteins.

Question 7

Which of the following is true regarding the structure shown? -CH₂-CH₂-COO-

Accepted Answer

A) Side chain of glutamine; normally found in the interior of globular proteins. 
B) Side chain of glutamine; normally found on the surface of globular proteins. 
C) Side chain of glutamate; normally found in the interior of globular proteins. 
D) Side chain of glutamate; normally found on the surface of globular proteins. 
E) Side chain of the "nonstandard" amino acid g-carboxyglutamate, found only in some clotting factors. 
A) Side chain of glutamine; normally found in the interior of globular proteins. 
B) Side chain of glutamine; normally found on the surface of globular proteins. 
C) Side chain of glutamate; normally found in the interior of globular proteins. 
D) Side chain of glutamate; normally found on the surface of globular proteins. 
E) Side chain of the "nonstandard" amino acid g-carboxyglutamate, found only in some clotting factors.

Question 8

Which of the following statements about protein structure is correct?

Accepted Answer

A) The helix is stabilized primarily by ionic interactions between the side chains of amino acids. 
B) Cytoplasmic proteins generally contain disulfide bonds. 
C) In comparison with the b-pleated sheet, the a helix is more extended. 
D) The denaturation of proteins is in most cases reversible by slow cooling. 
E) The tertiary structure of the protein forms before the formation of disulfide bonds. 
A) The helix is stabilized primarily by ionic interactions between the side chains of amino acids. 
B) Cytoplasmic proteins generally contain disulfide bonds. 
C) In comparison with the b-pleated sheet, the a helix is more extended. 
D) The denaturation of proteins is in most cases reversible by slow cooling. 
E) The tertiary structure of the protein forms before the formation of disulfide bonds.

Question 9

In the tripeptide glutathione (γ-glutamyl-cysteinyl-glycine), the side chain carboxyl group of glutamate forms a peptide bond with the α-amino group of cysteine.The α-amino and α-carboxyl groups of glutamate do not participate in peptide bonds.Approximately what is the isoelectric point (pK) of glutathione?

Accepted Answer

A) 1.5. 
B) 10.0. 
C) 3.0. 
D) 6.5. 
E) 9.0. 
A) 1.5. 
B) 10.0. 
C) 3.0. 
D) 6.5. 
E) 9.0.

Question 10

An amino acid whose side chain is most likely to be found in the center of a tightly packed, water-soluble globular protein such as myoglobin is:

Accepted Answer

A) Serine. 
B) Glutamine. 
C) Aspartate. 
D) Leucine. 
E) Arginine. 
A) Serine. 
B) Glutamine. 
C) Aspartate. 
D) Leucine. 
E) Arginine.

Question 11

Which amino acid residues are used as attachment sites for covalently bound oligosaccharides in glycoproteins?

Accepted Answer

A) Asparagine and serine. 
B) Tryptophan and glutamic acid. 
C) Alanine and lysine. 
D) Arginine and proline. 
E) Leucine and histidine. 
A) Asparagine and serine. 
B) Tryptophan and glutamic acid. 
C) Alanine and lysine. 
D) Arginine and proline. 
E) Leucine and histidine.

Question 12

Which of the following is true about the tertiary structure of proteins?

Accepted Answer

A) Disulfide bonds are part of the tertiary structure. 
B) Only proteins with more than one polypeptide subunit have a tertiary structure. 
C) Proteins with tertiary structure do not contain α helix or β-pleated sheet. 
D) Van der Waals interactions play no role in the tertiary structure. 
E) Interactions between hydrophobic amino acid side chains are important for hold the tertiary structure together. 
A) Disulfide bonds are part of the tertiary structure. 
B) Only proteins with more than one polypeptide subunit have a tertiary structure. 
C) Proteins with tertiary structure do not contain α helix or β-pleated sheet. 
D) Van der Waals interactions play no role in the tertiary structure. 
E) Interactions between hydrophobic amino acid side chains are important for hold the tertiary structure together.

Exam 2: Introduction to Protein Structure

Noncovalent bonds essential for the formation of the α helix and b-pleated sheet are:

Histones are proteins that bind to negatively charged phosphate groups of DNA.An amino acid in the histones that can mediate this binding is:

Amino acids at the isoelectric point in the titration curve have a net charge of:

Which of the following statements is correct for protein structure?

All naturally occurring amino acids:

The secondary structure of proteins:

Which of the following is true regarding the structure shown? -CH₂-CH₂-COO-

Which of the following statements about protein structure is correct?

An amino acid whose side chain is most likely to be found in the center of a tightly packed, water-soluble globular protein such as myoglobin is:

Which amino acid residues are used as attachment sites for covalently bound oligosaccharides in glycoproteins?

Which of the following is true about the tertiary structure of proteins?

Introduction to Biomolecules

Oxygen Transporters: Hemoglobin and Myoglobin

Enzymatic Reactions

Coenzymes

DNA, RNA, and Protein Synthesis

The Human Genome

Protein Targeting

Introduction to Genetic Diseases

Viruses

DNA Technology

Biological Membranes

The Cytoskeleton

The Extracellular Matrix

Plasma Proteins

Extracellular Messengers

Intracellular Messengers

Cellular Growth Control and Cancer

Digestive Enzymes

Introduction to Metabolic Pathways

Glycolysis, Tricarboxylic Acid Cycle, and Oxidative Phosphorylation

Carbohydrate Metabolism

The Metabolism of Fatty Acids and Triglycerides

The Metabolism of Membrane Lipids

Lipid Transport

Amino Acid Metabolism

Heme Metabolism

The Metabolism of Purines and Pyrimidines

Vitamins and Minerals

Integration of Metabolism

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