Question 1

The carbon with the asterisk next to it is called the

Accepted Answer

A)  anomeric carbon. 
B)  alpha carbon. 
C)  beta carbon. 
D)  gamma carbon. 
E)  side-chain carbon. 
A)  anomeric carbon. 
B)  alpha carbon. 
C)  beta carbon. 
D)  gamma carbon. 
E)  side-chain carbon.

Question 2

The carbon with a smiley face over it is a(n)

Accepted Answer

A)  beta carbon. 
B)  anomeric carbon. 
C)  chirality center. 
D)  secondary amine. 
E)  peptide bond. 
A)  beta carbon. 
B)  anomeric carbon. 
C)  chirality center. 
D)  secondary amine. 
E)  peptide bond.

Question 3

An amino acid substitution can result in a large change in secondary and tertiary structure.Sometimes, the substitution leads to very little change.The structure of valine is shown below.Which amino acid would probably cause the least amount of perturbation to protein structure if it was substituted for a valine?

Accepted Answer

A)  amino acid a 
B)  amino acid b 
C)  amino acid c 
D)  amino acid d 
E)  amino acid e 
A)  amino acid a 
B)  amino acid b 
C)  amino acid c 
D)  amino acid d 
E)  amino acid e

Question 4

The pH for optimum activity for most enzymes is

Accepted Answer

A)  5.4. 
B)  7.4. 
C)  8.0. 
D)  9.0. 
E)  10.4. 
A)  5.4. 
B)  7.4. 
C)  8.0. 
D)  9.0. 
E)  10.4.

Question 5

Which statement BEST describes the strategy used for treating hypertension through drug therapies?

Accepted Answer

A)  to suppress how the body detects sodium 
B)  to suppress how the body detects low blood pressure 
C)  to lower blood pressure directly 
D)  to permanently disable renin 
E)  to inhibit the pathway that the body uses to increase blood pressure 
A)  to suppress how the body detects sodium 
B)  to suppress how the body detects low blood pressure 
C)  to lower blood pressure directly 
D)  to permanently disable renin 
E)  to inhibit the pathway that the body uses to increase blood pressure

Question 6

The structure of lysine is shown below.What is the overall charge on lysine at physiological pH?

Accepted Answer

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

Question 7

Which statement BEST describes the function of an enzyme in the body?

Accepted Answer

A)  An enzyme acts as a buffer. 
B)  An enzyme transports waste out of the blood. 
C)  An enzyme signals cellular events. 
D)  An enzyme catalyzes chemical reactions. 
E)  All of the above describe the function. 
A)  An enzyme acts as a buffer. 
B)  An enzyme transports waste out of the blood. 
C)  An enzyme signals cellular events. 
D)  An enzyme catalyzes chemical reactions. 
E)  All of the above describe the function.

Question 8

Which of the amino acids does NOT contain a chiral carbon?

Accepted Answer

A)  amino acid a 
B)  amino acid b 
C)  amino acid c 
D)  amino acid d 
E)  amino acid e 
A)  amino acid a 
B)  amino acid b 
C)  amino acid c 
D)  amino acid d 
E)  amino acid e

Question 9

The structure of myoglobin is shown below.Which level of architecture does this protein lack?

Accepted Answer

A)  This protein has all levels of architecture. 
B)  primary 
C)  secondary 
D)  tertiary 
E)  quaternary 
A)  This protein has all levels of architecture. 
B)  primary 
C)  secondary 
D)  tertiary 
E)  quaternary

Question 10

Why doesn't denaturation affect the primary structure of a protein?

Accepted Answer

A)  Actually, denaturation does hydrolyze amino acids. 
B)  Peptide bonds are higher energy bonds than other interactions. 
C)  Peptide bonds are stronger than other interactions. 
D)  Peptide bonds are weaker than other interactions. 
E)  Peptide bonds cannot be broken under any circumstances. 
A)  Actually, denaturation does hydrolyze amino acids. 
B)  Peptide bonds are higher energy bonds than other interactions. 
C)  Peptide bonds are stronger than other interactions. 
D)  Peptide bonds are weaker than other interactions. 
E)  Peptide bonds cannot be broken under any circumstances.

Question 11

The following is a description of an enzyme called superoxide dismutase.Refer to this paragraph to answer the following question. Superoxide dismutase is an enzyme that detoxifies a free radical called superoxide.This radical is responsible for causing injury during reperfusion after a heart attack, and is also thought to play a role in Parkinson's Disease.a Depending on what organism the protein is found in, it occurs either as a dimer or tetramer of identical subunits.b The subunits are mostly α-helical with some β-sheet near the C-terminus.c A metal binding site for manganese, iron, nickel or copper/zinc is composed of residues from both the N-terminus and the C-terminus.d These residues are: His-26, His-81, Asp-167, His-171.e
Which statement refers to quaternary structure?

Accepted Answer

A)  statement a 
B)  statement b 
C)  statement c 
D)  statement d 
E)  statement e 
A)  statement a 
B)  statement b 
C)  statement c 
D)  statement d 
E)  statement e

Question 12

Prion disease is a disease of the ________________ protein structure.

Accepted Answer

A)  primary 
B)  secondary 
C)  tertiary 
D)  quaternary 
E)  Prion disease does not involve proteins. 
A)  primary 
B)  secondary 
C)  tertiary 
D)  quaternary 
E)  Prion disease does not involve proteins.

Question 13

Assuming that the enzyme represented by the graph below is found in humans, what temperature is MOST likely to be the optimum temperature?

Accepted Answer

A)  0 ºC 
B)  10 ºC 
C)  37 ºC 
D)  55 ºC 
E)  100 ºC 
A)  0 ºC 
B)  10 ºC 
C)  37 ºC 
D)  55 ºC 
E)  100 ºC

Question 14

According to the graph below, which of the following is TRUE?

Accepted Answer

A)  At high temperature, the activity of the enzyme decreases more sharply than it does at low temperature. 
B)  At low temperature, the activity of the enzyme decreases more sharply than it does at high temperature. 
C)  The maximum activity is at the lowest temperature. 
D)  The maximum activity is at the highest temperature. 
E)  The activity of the enzyme is the same at all temperatures. 
A)  At high temperature, the activity of the enzyme decreases more sharply than it does at low temperature. 
B)  At low temperature, the activity of the enzyme decreases more sharply than it does at high temperature. 
C)  The maximum activity is at the lowest temperature. 
D)  The maximum activity is at the highest temperature. 
E)  The activity of the enzyme is the same at all temperatures.

Question 15

What percentage of amino acids in sickle-cell hemoglobin is different from normal hemoglobin?

Accepted Answer

A)  100% 
B)  50% 
C)  25% 
D)  10% 
E)  < 1% 
A)  100% 
B)  50% 
C)  25% 
D)  10% 
E)  < 1%

Question 16

Which statement BEST describes prosthetic groups?

Accepted Answer

A)  They are nonpeptide molecules or ions essential to a protein's structure. 
B)  They are short peptide chains attached to a larger protein. 
C)  They are nonfunctional components of a protein. 
D)  They are the active part of a protein. 
E)  They are the part of the protein that provides structure. 
A)  They are nonpeptide molecules or ions essential to a protein's structure. 
B)  They are short peptide chains attached to a larger protein. 
C)  They are nonfunctional components of a protein. 
D)  They are the active part of a protein. 
E)  They are the part of the protein that provides structure.

Question 17

Amino acids that are not synthesized in the body and must be obtained from the diet are called

Accepted Answer

A)  nonpolar. 
B)  incomplete. 
C)  necessary. 
D)  essential. 
E)  edible. 
A)  nonpolar. 
B)  incomplete. 
C)  necessary. 
D)  essential. 
E)  edible.

Question 18

The following amino acid is classified as nonpolar.Which statement BEST describes why it is classified this way?

Accepted Answer

A)  It does not form a zwitterion. 
B)  It is neutral at physiological pH. 
C)  Its side chain is not charged at physiological pH. 
D)  Its side chain is a hydrocarbon. 
E)  This amino acid is soluble only in nonpolar solvents. 
A)  It does not form a zwitterion. 
B)  It is neutral at physiological pH. 
C)  Its side chain is not charged at physiological pH. 
D)  Its side chain is a hydrocarbon. 
E)  This amino acid is soluble only in nonpolar solvents.

Question 19

About how many different proteins are in the human body?

Accepted Answer

A)  one hundred 
B)  one thousand 
C)  ten thousand 
D)  one hundred thousand 
E)  one million 
A)  one hundred 
B)  one thousand 
C)  ten thousand 
D)  one hundred thousand 
E)  one million

Question 20

These proteins are structural in nature.

Accepted Answer

A)  keratin 
B)  keratin, elastin, and collagen 
C)  membrane proteins and globular proteins 
D)  globular proteins 
E)  membrane proteins 
A)  keratin 
B)  keratin, elastin, and collagen 
C)  membrane proteins and globular proteins 
D)  globular proteins 
E)  membrane proteins

The carbon with the asterisk next to it is called the

The carbon with a smiley face over it is a(n)

The pH for optimum activity for most enzymes is

Which statement BEST describes the strategy used for treating hypertension through drug therapies?

The structure of lysine is shown below.What is the overall charge on lysine at physiological pH?

Which statement BEST describes the function of an enzyme in the body?

Which of the amino acids does NOT contain a chiral carbon?

The structure of myoglobin is shown below.Which level of architecture does this protein lack?

Why doesn't denaturation affect the primary structure of a protein?

Prion disease is a disease of the ________________ protein structure.

Assuming that the enzyme represented by the graph below is found in humans, what temperature is MOST likely to be the optimum temperature?

According to the graph below, which of the following is TRUE?

What percentage of amino acids in sickle-cell hemoglobin is different from normal hemoglobin?

Which statement BEST describes prosthetic groups?

Amino acids that are not synthesized in the body and must be obtained from the diet are called

The following amino acid is classified as nonpolar.Which statement BEST describes why it is classified this way?

About how many different proteins are in the human body?

These proteins are structural in nature.

Matter, Energy, and Measurement

Atomic Structure and Radioisotopes

Ionic and Covalent Compounds

Molecular Geometry, Polarity, and Intermolecular

Chemical Quantities and Introduction to Reactions

Chemical Reactions: Energy, Rates, and Equilibrium

Changes of State and Gas Laws

Mixtures, Solution Concentrations, and Diffusion

Acids and Bases, Ph, and Buffers

Introduction to Organic Chemistry:

Alcohols, Phenols, Thiols, Ethers, and Amines

The Carbonyl Containing Functional Groups

The Common Organic Reactions in Biochemistry

Carbohydrates: Structure and Function

Lipids: Structure and Function

Nucleotides and Nucleic Acids

Energy and Metabolism

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Exam 16: Proteins: Structure and Function

The carbon with the asterisk next to it is called the

The carbon with a smiley face over it is a(n)

The pH for optimum activity for most enzymes is

Which statement BEST describes the strategy used for treating hypertension through drug therapies?

The structure of lysine is shown below.What is the overall charge on lysine at physiological pH?

Which statement BEST describes the function of an enzyme in the body?

Which of the amino acids does NOT contain a chiral carbon?

The structure of myoglobin is shown below.Which level of architecture does this protein lack?

Why doesn't denaturation affect the primary structure of a protein?

Prion disease is a disease of the ________________ protein structure.

Assuming that the enzyme represented by the graph below is found in humans, what temperature is MOST likely to be the optimum temperature?

According to the graph below, which of the following is TRUE?

What percentage of amino acids in sickle-cell hemoglobin is different from normal hemoglobin?

Which statement BEST describes prosthetic groups?

Amino acids that are not synthesized in the body and must be obtained from the diet are called

The following amino acid is classified as nonpolar.Which statement BEST describes why it is classified this way?

About how many different proteins are in the human body?

These proteins are structural in nature.

Matter, Energy, and Measurement

Atomic Structure and Radioisotopes

Ionic and Covalent Compounds

Molecular Geometry, Polarity, and Intermolecular

Chemical Quantities and Introduction to Reactions

Chemical Reactions: Energy, Rates, and Equilibrium

Changes of State and Gas Laws

Mixtures, Solution Concentrations, and Diffusion

Acids and Bases, Ph, and Buffers

Introduction to Organic Chemistry:

Alcohols, Phenols, Thiols, Ethers, and Amines

The Carbonyl Containing Functional Groups

The Common Organic Reactions in Biochemistry

Carbohydrates: Structure and Function

Lipids: Structure and Function

Nucleotides and Nucleic Acids

Energy and Metabolism

Filters