Question 1

Exhibit 4A The following question(s) refer to this peptide:
Cys-Ala-Gly-Arg-Gln-Met
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. D

Question 2

Exhibit 4A The following question(s) refer to this peptide:
Cys-Ala-Gly-Arg-Gln-Met
Refer to Exhibit 4A.The amino terminal amino acid 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. B

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

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 5

Incorrect protein folding resulting in exposure of hydrophobic regions can result in

Accepted Answer

A)  aggregation. 
B)  homology. 
C)  liposomes. 
D)  the Bohr effect. 
A)  aggregation. 
B)  homology. 
C)  liposomes. 
D)  the Bohr effect.

Question 6

Exhibit 4A The following question(s) refer to this peptide:
Cys-Ala-Gly-Arg-Gln-Met
Refer to Exhibit 4A.The overall,net ionic charge on this peptide at pH = 7 would be:

Accepted Answer

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

Question 7

The following is true about the hydroxyproline in collagen:

Accepted Answer

A)  Hydroxyproline is incorporated into the chain during polymerization of amino acids. 
B)  Vitamin C is necessary for the synthesis of hydroxyproline. 
C)  Hydroxyproline is important in holding the 3 strands of collagen together. 
D)  Hydroxyproline requires Vitamin C for its synthesis and it holds the collagen helix together. 
E)  All of these. 
A)  Hydroxyproline is incorporated into the chain during polymerization of amino acids. 
B)  Vitamin C is necessary for the synthesis of hydroxyproline. 
C)  Hydroxyproline is important in holding the 3 strands of collagen together. 
D)  Hydroxyproline requires Vitamin C for its synthesis and it holds the collagen helix together. 
E)  All of these.

Question 8

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

Question 9

Under normal circumstances:

Accepted Answer

A)  Adult Hb binds to oxygen more tightly than Mb binds. 
B)  Fetal Hb binds oxygen more tightly than adult Hb. 
C)  Adult Hb binds oxygen more tightly than either fetal Hb or Mb binds. 
D)  Mb has the lowest affinity for oxygen of the 3. 
E)  More than one of these statements is correct. 
A)  Adult Hb binds to oxygen more tightly than Mb binds. 
B)  Fetal Hb binds oxygen more tightly than adult Hb. 
C)  Adult Hb binds oxygen more tightly than either fetal Hb or Mb binds. 
D)  Mb has the lowest affinity for oxygen of the 3. 
E)  More than one of these statements is correct.

Question 10

The protein myoglobin

Accepted Answer

A)  contains a high degree of b-pleated sheet structure 
B)  carries oxygen in the bloodstream 
C)  contains no histidine 
D)  contains a heme group 
A)  contains a high degree of b-pleated sheet structure 
B)  carries oxygen in the bloodstream 
C)  contains no histidine 
D)  contains a heme group

Question 11

Which of the following best defines a domain?

Accepted Answer

A)  A supersecondary region, often shared by proteins, that has a specific function. 
B)  A repetitive supersecondary structure. 
C)  A double-layered arrangement formed so that the polar groups face the aqueous environment, while the nonpolar regions are kept away from the aqueous environment. 
D)  An unfolded region of a protein. 
A)  A supersecondary region, often shared by proteins, that has a specific function. 
B)  A repetitive supersecondary structure. 
C)  A double-layered arrangement formed so that the polar groups face the aqueous environment, while the nonpolar regions are kept away from the aqueous environment. 
D)  An unfolded region of a protein.

Question 12

Structures which repeat over and over in secondary structure are called:

Accepted Answer

A)  primary structure 
B)  domain 
C)  supersecondary structure 
D)  prosthetic group 
E)  All of these 
A)  primary structure 
B)  domain 
C)  supersecondary structure 
D)  prosthetic group 
E)  All of these

Question 13

The Bohr effect for oxygen binding states that

Accepted Answer

A)  Mb binds oxygen more tightly than Hb. 
B)  Hb will bind oxygen very tightly when the CO2 concentration is high. 
C)  as the pH goes down, Hb binds oxygen less tightly. 
D)  Hb's ability to bind oxygen increases with higher oxygen concentration. 
A)  Mb binds oxygen more tightly than Hb. 
B)  Hb will bind oxygen very tightly when the CO2 concentration is high. 
C)  as the pH goes down, Hb binds oxygen less tightly. 
D)  Hb's ability to bind oxygen increases with higher oxygen concentration.

Question 14

Which of the following is not a characteristic of hemoglobin?

Accepted Answer

A)  It contains two different types of subunits . 
B)  It contains a prosthetic group. 
C)  It is an allosteric enzyme. 
D)  It transports oxygen. 
E)  All of these statements are true for Hb. 
A)  It contains two different types of subunits . 
B)  It contains a prosthetic group. 
C)  It is an allosteric enzyme. 
D)  It transports oxygen. 
E)  All of these statements are true for Hb.

Question 15

Exhibit 4A The following question(s) refer to this peptide:
Cys-Ala-Gly-Arg-Gln-Met
Refer to Exhibit 4A.Total hydrolysis of the peptide in HCl would yield these products:

Accepted Answer

A)  Ala, Arg, Cys, Gln, Gly, Met 
B)  Ala, Arg, 2 Cys, Gln, Gly, H2S 
C)  Ala, Arg, Cys, Glu, Gly, Met, NH3 
D)  Ala, Arg, 2 Cys, Glu, Gly, H2S, NH3 
E)  None of these answers is correct. 
A)  Ala, Arg, Cys, Gln, Gly, Met 
B)  Ala, Arg, 2 Cys, Gln, Gly, H2S 
C)  Ala, Arg, Cys, Glu, Gly, Met, NH3 
D)  Ala, Arg, 2 Cys, Glu, Gly, H2S, NH3 
E)  None of these answers is correct.

Question 16

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 17

Which one is not an example of supersecondary structure?

Accepted Answer

A)  the pyrrole ring 
B)  the Greek key 
C)  the b-meander 
D)  the b-barrel 
A)  the pyrrole ring 
B)  the Greek key 
C)  the b-meander 
D)  the b-barrel

Question 18

Disulfide bonds in proteins occur between the side chains of which of the following amino acid residues?

Accepted Answer

A)  glutamine 
B)  lysine 
C)  cysteine 
D)  methionine 
A)  glutamine 
B)  lysine 
C)  cysteine 
D)  methionine

Question 19

Covalent bonds are important in all these structures,except:

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 20

Quaternary structure is associated with

Accepted Answer

A)  the overall shape of the polypeptide chain 
B)  the sum of secondary and tertiary interactions 
C)  simple proteins with only one subunit 
D)  the relative orientation of one polypeptide to another polypeptide in a multisubunit protein 
A)  the overall shape of the polypeptide chain 
B)  the sum of secondary and tertiary interactions 
C)  simple proteins with only one subunit 
D)  the relative orientation of one polypeptide to another polypeptide in a multisubunit protein

Exam 4: The Three-Dimensional Structure of Proteins

Exhibit 4A The following question(s) refer to this peptide: Cys-Ala-Gly-Arg-Gln-Met Refer to Exhibit 4A.The carboxyl terminal end is:

Exhibit 4A The following question(s) refer to this peptide: Cys-Ala-Gly-Arg-Gln-Met Refer to Exhibit 4A.The amino terminal amino acid is:

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

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

Incorrect protein folding resulting in exposure of hydrophobic regions can result in

Exhibit 4A The following question(s) refer to this peptide: Cys-Ala-Gly-Arg-Gln-Met Refer to Exhibit 4A.The overall,net ionic charge on this peptide at pH = 7 would be:

The following is true about the hydroxyproline in collagen:

In sickle-cell anemia hemoglobin

Under normal circumstances:

The protein myoglobin

Which of the following best defines a domain?

Structures which repeat over and over in secondary structure are called:

The Bohr effect for oxygen binding states that

Which of the following is not a characteristic of hemoglobin?

Exhibit 4A The following question(s) refer to this peptide: Cys-Ala-Gly-Arg-Gln-Met Refer to Exhibit 4A.Total hydrolysis of the peptide in HCl would yield these products:

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

Which one is not an example of supersecondary structure?

Disulfide bonds in proteins occur between the side chains of which of the following amino acid residues?

Covalent bonds are important in all these structures,except:

Quaternary structure is associated with

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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