Question 1

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 2

The three-dimensional shapes of proteins with biological activities are called _____.

Accepted Answer

A)  prosthetic groups 
B)  subunits 
C)  native conformations 
D)  domains 
A)  prosthetic groups 
B)  subunits 
C)  native conformations 
D)  domains

Question 3

A single amino substitution can give rise to a malfunctioning protein.

Accepted Answer

A) True 
 B)False

Question 4

Adult hemoglobin is half saturated with oxygen at what partial pressure of oxygen?

Accepted Answer

A)  5 torr 
B)  10 torr 
C)  25 torr 
D)  50 torr 
E)  100 torr 
A)  5 torr 
B)  10 torr 
C)  25 torr 
D)  50 torr 
E)  100 torr

Question 5

Hemoglobin differs from myoglobin because

Accepted Answer

A)  it does not have a heme group. 
B)  it is a tetramer, whereas myoglobin is a single polypeptide chain. 
C)  it does not contain any helical regions. 
D)  it contains more β -pleated sheet structure. 
A)  it does not have a heme group. 
B)  it is a tetramer, whereas myoglobin is a single polypeptide chain. 
C)  it does not contain any helical regions. 
D)  it contains more β -pleated sheet structure.

Question 6

The structure of myoglobin consists

Accepted Answer

A)  almost entirely of α -helices. 
B)  almost entirely of β -sheets. 
C)  of a mixture of α -helices and β -sheets. 
D)  of a unique secondary motif that is neither α -helix nor β -sheet. 
A)  almost entirely of α -helices. 
B)  almost entirely of β -sheets. 
C)  of a mixture of α -helices and β -sheets. 
D)  of a unique secondary motif that is neither α -helix nor β -sheet.

Question 7

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 8

Domains are

Accepted Answer

A)  independently folded regions of proteins 
B)  the α -helical portions of proteins 
C)  the β -pleated regions of proteins 
D)  all of the above 
A)  independently folded regions of proteins 
B)  the α -helical portions of proteins 
C)  the β -pleated regions of proteins 
D)  all of the above

Question 9

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 10

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 11

Match between columns
                        Premises:  The arrangement of space of the backbone atoms in a polypeptide chain
 The order in which the amino acids in a protein are linked by peptide bonds
 The interaction of several polypeptide chains in a multisubunit protein
 Specific clusters of secondary structural motifs in proteins
 The arrangement in space of all the atoms in a protein

Accepted Answer

The Answer of Secondary structure and Quaternary structure and Tertiary is...

Question 12

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 13

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 14

Which of the following amino acid substitutions would be least likely to have a deleterious effect on protein function?

Accepted Answer

A)  His changes to Asp 
B)  Leu changes to Ile 
C)  Glu changes to Gln 
D)  Trp changes to Gly 
A)  His changes to Asp 
B)  Leu changes to Ile 
C)  Glu changes to Gln 
D)  Trp changes to Gly

Question 15

In what oxidation state must the iron atom be for heme to bind oxygen?

Accepted Answer

A)  0, Fe(0) 
B)  1+, Fe(I) 
C)  2+, Fe(II) 
D)  3+, Fe(III) 
E)  There is no required oxidation state for the iron. 
A)  0, Fe(0) 
B)  1+, Fe(I) 
C)  2+, Fe(II) 
D)  3+, Fe(III) 
E)  There is no required oxidation state for the iron.

Question 16

Which of the following is true about the alpha helix?

Accepted Answer

A)  the structure is stablized by hydrogen bonds 
B)  there are 3.6 residues for every turn of the helix 
C)  the pitch of the helix is 5.4 angsroms 
D)  all of the choices 
A)  the structure is stablized by hydrogen bonds 
B)  there are 3.6 residues for every turn of the helix 
C)  the pitch of the helix is 5.4 angsroms 
D)  all of the choices

Question 17

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

Question 18

The protein myoglobin

Accepted Answer

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

Question 19

In the β -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 20

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)

Exam 4: The Three Dimensional Structure of Proteins

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

The three-dimensional shapes of proteins with biological activities are called _____.

A single amino substitution can give rise to a malfunctioning protein.

Adult hemoglobin is half saturated with oxygen at what partial pressure of oxygen?

Hemoglobin differs from myoglobin because

The structure of myoglobin consists

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

Domains are

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

In sickle-cell anemia hemoglobin

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

Heme would best be described as a

Which of the following amino acid substitutions would be least likely to have a deleterious effect on protein function?

In what oxidation state must the iron atom be for heme to bind oxygen?

Which of the following is true about the alpha helix?

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

The protein myoglobin

In the β -pleated sheet conformation

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

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 the 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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