Question 1

Which of the following pairs of elements are present in proteins,but not in most carbohydrates?

Accepted Answer

A) nitrogen and sulfur 
B) carbon and hydrogen 
C) carbon and oxygen 
D) sulfur and oxygen 
E) nitrogen and oxygen 
A) nitrogen and sulfur 
B) carbon and hydrogen 
C) carbon and oxygen 
D) sulfur and oxygen 
E) nitrogen and oxygen

Question 2

Proteins that are insoluble in water are called globular.

Accepted Answer

A) True 
 B)False

Question 3

Which of the following best describes where the amino acids isoleucine and tryptophan are most likely to be found in the tertiary structure of a protein?

Accepted Answer

A) at the N-terminal end of the protein 
B) at the C-terminal end of the protein 
C) on the exterior surface of the folded protein where contact with water is greatest,due to their hydrophilic nature 
D) in the interior of the folded protein away from water,due to their hydrophobic nature 
E) in the hydrophilic interior of the protein due to their ability to form side chain hydrogen bonds with each other 
A) at the N-terminal end of the protein 
B) at the C-terminal end of the protein 
C) on the exterior surface of the folded protein where contact with water is greatest,due to their hydrophilic nature 
D) in the interior of the folded protein away from water,due to their hydrophobic nature 
E) in the hydrophilic interior of the protein due to their ability to form side chain hydrogen bonds with each other

Question 4

How many different amino acids make up the proteins found in the human body?

Accepted Answer

A) 4 
B) 16 
C) 20 
D) 125 
E) This has not yet been determined. 
A) 4 
B) 16 
C) 20 
D) 125 
E) This has not yet been determined.

Question 5

What is the term for the state of a protein when its organized structure has become completely disorganized?

Accepted Answer

A) hydrolyzed 
B) isomerized 
C) globular 
D) denatured 
E) fibrous 
A) hydrolyzed 
B) isomerized 
C) globular 
D) denatured 
E) fibrous

Question 6

The properties of amino acids and the proteins they compose are based on the nature of their side chain group.Which term best classifies the side chain of the amino acid phenylalanine?

Accepted Answer

A) basic 
B) acidic 
C) nonpolar,hydrophobic 
D) polar,neutral 
E) polar,hydrophilic 
A) basic 
B) acidic 
C) nonpolar,hydrophobic 
D) polar,neutral 
E) polar,hydrophilic

Question 7

Which amino acid contains a thiol in its R group?

Accepted Answer

A) methionine 
B) alanine 
C) cysteine 
D) tyrosine 
E) valine 
A) methionine 
B) alanine 
C) cysteine 
D) tyrosine 
E) valine

Question 8

Proteins are long chains of amino acids joined together by peptide bonds.Which of the following properly depicts the peptide bond formed between two generic amino acids?

Accepted Answer

A) 
  
B) 
  
C) 
  
D) 
  
E) 
  
A) 
  
B) 
  
C) 
  
D) 
  
E)

Question 9

Tuftsin is a peptide that stimulates and promotes the destruction of tumor cells.Its primary structure is shown below.Which of the following is NOT a valid interpretation of its primary structure? Thr-Lys-Pro-Arg

Accepted Answer

A) It is a tetrapeptide. 
B) It contains three peptide bonds. 
C) Threonine is the N-terminal amino acid and arginine is the C-terminal amino acid. 
D) The carboxyl group of lysine is joined to the amino group of proline. 
E) The amino group of arginine is not joined to any other amino acid. 
A) It is a tetrapeptide. 
B) It contains three peptide bonds. 
C) Threonine is the N-terminal amino acid and arginine is the C-terminal amino acid. 
D) The carboxyl group of lysine is joined to the amino group of proline. 
E) The amino group of arginine is not joined to any other amino acid.

Question 10

2-Amino-4-methylpentanoic acid (common name leucine)is an essential amino acid found in the proteins of the human body.Which of the following properly represents the structure of this compound?

Accepted Answer

A) 
  
B) 
  
C) 
  
D) 
  
E) 
  
A) 
  
B) 
  
C) 
  
D) 
  
E)

Question 11

Which of the following is a structural protein?

Accepted Answer

A) albumin 
B) keratin 
C) insulin 
D) trypsin 
E) myoglobin 
A) albumin 
B) keratin 
C) insulin 
D) trypsin 
E) myoglobin

Question 12

What essential type of reaction of collagen requires the presence of vitamin C before it will occur?

Accepted Answer

A) hydration 
B) hydrolysis 
C) hydrogenation 
D) hydroxylation 
E) peptidation 
A) hydration 
B) hydrolysis 
C) hydrogenation 
D) hydroxylation 
E) peptidation

Question 13

The human body can synthesize nonessential amino acids,but not essential ones.

Accepted Answer

A) True 
 B)False

Question 14

What protein is the oxygen storage protein of the skeletal muscles?

Accepted Answer

A) insulin 
B) collagen 
C) myoglobin 
D) albumin 
E) hemoglobin 
A) insulin 
B) collagen 
C) myoglobin 
D) albumin 
E) hemoglobin

Question 15

Glycoproteins are often found as receptors on the surface of cells.

Accepted Answer

A) True 
 B)False

Question 16

What is meant by the "quaternary structure" of a protein?

Accepted Answer

A) It refers to the four atoms that make up the peptide bonds that join the amino acids together in the protein chain. 
B) It describes the unique sequence of four amino acids in the protein chain. 
C) It describes the four regular,repeating structures found in the protein chain. 
D) It describes the overall three dimensional shape of a protein. 
E) It describes the association of two or more polypeptide chains to form one functioning protein unit. 
A) It refers to the four atoms that make up the peptide bonds that join the amino acids together in the protein chain. 
B) It describes the unique sequence of four amino acids in the protein chain. 
C) It describes the four regular,repeating structures found in the protein chain. 
D) It describes the overall three dimensional shape of a protein. 
E) It describes the association of two or more polypeptide chains to form one functioning protein unit.

Question 17

How do the primary structures of normal hemoglobin and sickle cell hemoglobin differ?

Accepted Answer

A) A glutamic acid residue in normal hemoglobin is replaced by a valine residue in sickle cell hemoglobin. 
B) A valine acid residue in normal hemoglobin is replaced by a glutamic acid residue in sickle cell hemoglobin. 
C) There are four heme groups in normal hemoglobin whereas there are only three heme groups in sickle cell hemoglobin. 
D) There are three heme groups in normal hemoglobin whereas there are 4 heme groups in sickle cell hemoglobin. 
E) Both A and C are correct. 
A) A glutamic acid residue in normal hemoglobin is replaced by a valine residue in sickle cell hemoglobin. 
B) A valine acid residue in normal hemoglobin is replaced by a glutamic acid residue in sickle cell hemoglobin. 
C) There are four heme groups in normal hemoglobin whereas there are only three heme groups in sickle cell hemoglobin. 
D) There are three heme groups in normal hemoglobin whereas there are 4 heme groups in sickle cell hemoglobin. 
E) Both A and C are correct.

Question 18

How many oxygen molecules can one hemoglobin molecule bind?

Accepted Answer

A) 1 
B) 2 
C) 3 
D) 4 
E) 5 
A) 1 
B) 2 
C) 3 
D) 4 
E) 5

Question 19

The formation of a peptide bond is best described as which of the following?

Accepted Answer

A) neutralization reaction 
B) dehydration reaction 
C) hydration reaction 
D) hydrogenation reaction 
E) oxidation reaction 
A) neutralization reaction 
B) dehydration reaction 
C) hydration reaction 
D) hydrogenation reaction 
E) oxidation reaction

Question 20

How is the following amino acid categorized? The structure shows its form at pH = 7.

Accepted Answer

A) hydrophobic 
B) polar,acidic 
C) polar,basic 
D) polar,neutral 
E) None of the choices are correct. 
A) hydrophobic 
B) polar,acidic 
C) polar,basic 
D) polar,neutral 
E) None of the choices are correct.

Exam 18: Protein Structure and Function

Which of the following pairs of elements are present in proteins,but not in most carbohydrates?

Proteins that are insoluble in water are called globular.

Which of the following best describes where the amino acids isoleucine and tryptophan are most likely to be found in the tertiary structure of a protein?

How many different amino acids make up the proteins found in the human body?

What is the term for the state of a protein when its organized structure has become completely disorganized?

The properties of amino acids and the proteins they compose are based on the nature of their side chain group.Which term best classifies the side chain of the amino acid phenylalanine?

Which amino acid contains a thiol in its R group?

Proteins are long chains of amino acids joined together by peptide bonds.Which of the following properly depicts the peptide bond formed between two generic amino acids?

Tuftsin is a peptide that stimulates and promotes the destruction of tumor cells.Its primary structure is shown below.Which of the following is NOT a valid interpretation of its primary structure? Thr-Lys-Pro-Arg

2-Amino-4-methylpentanoic acid (common name leucine)is an essential amino acid found in the proteins of the human body.Which of the following properly represents the structure of this compound?

Which of the following is a structural protein?

What essential type of reaction of collagen requires the presence of vitamin C before it will occur?

The human body can synthesize nonessential amino acids,but not essential ones.

What protein is the oxygen storage protein of the skeletal muscles?

Glycoproteins are often found as receptors on the surface of cells.

What is meant by the "quaternary structure" of a protein?

How do the primary structures of normal hemoglobin and sickle cell hemoglobin differ?

How many oxygen molecules can one hemoglobin molecule bind?

The formation of a peptide bond is best described as which of the following?

How is the following amino acid categorized? The structure shows its form at pH = 7.

Chemistry - Methods and Measurement

The Structure of the Atom and the Periodic Table

Structure and Properties of Ionic and Covalent Compounds

Calculations, chemical Changes, and the Chemical Equation

States of Matter: Gases, liquids, and Solids

Solutions

Energy,rate and Equilibrium

Acids and Bases

The Nucleus, radioactivity, and Nuclear Medicine

An Introduction to Organic Chemistry

The Unsaturated Hydrocarbons: Alkenes, alkynes, and Aromatics

Alcohols, phenols, thiols, and Ethers

Aldehydes and Ketones

Carboxylic Acids and Carboxylic Acid Derivatives

Amines and Amides

Carbohydrates

Lipids and Their Functions in Biochemical Systems

Enzymes

Introduction to Molecular Genetics

Carbohydrate Metabolism

Aerobic Respiration and Energy Production

Fatty Acid Metabolism

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