Question 1

In the peptide Ala-Try-Gly-Phe,the N-terminus is ________.

Accepted Answer

A) alanine 
B) phenylalanine 
C) tryptophan 
D) aspartate 
E) glycine 
A) alanine 
B) phenylalanine 
C) tryptophan 
D) aspartate 
E) glycine

Question 2

The optimum pH for the activity of pepsin is about ________.

Accepted Answer

A) 2.0 
B) 4.0 
C) 6.5 
D) 7.4 
E) 7.6 
A) 2.0 
B) 4.0 
C) 6.5 
D) 7.4 
E) 7.6

Question 3

The presence of enzymes to catalyze bioreactions in our bodies allows ________.

Accepted Answer

A) us to eat non-nutritious substances without consequence 
B) the activation energy of a reaction to be raised 
C) the rate of a desired chemical reaction to slow down 
D) bioreactions to occur under extreme conditions of temperature and pH 
E) bioreactions to take place under mild conditions 
A) us to eat non-nutritious substances without consequence 
B) the activation energy of a reaction to be raised 
C) the rate of a desired chemical reaction to slow down 
D) bioreactions to occur under extreme conditions of temperature and pH 
E) bioreactions to take place under mild conditions

Question 4

Heat denatures a protein by disrupting ________.

Accepted Answer

A) salt bridges and peptide bonds 
B) hydrophobic interactions and hydrogen bonds 
C) peptide bonds and hydrophobic interactions 
D) disulfide bonds and peptide bonds 
E) hydrogen bonds and disulfide bonds 
A) salt bridges and peptide bonds 
B) hydrophobic interactions and hydrogen bonds 
C) peptide bonds and hydrophobic interactions 
D) disulfide bonds and peptide bonds 
E) hydrogen bonds and disulfide bonds

Question 5

The one letter abbreviation for the amino acid tyrosine is ________.

Accepted Answer

A) T 
B) R 
C) Y 
D) W 
E) P 
A) T 
B) R 
C) Y 
D) W 
E) P

Question 6

Hemoglobin has a total of ________ protein chains in its quaternary structure.

Accepted Answer

A) one 
B) two 
C) three 
D) four 
E) five 
A) one 
B) two 
C) three 
D) four 
E) five

Question 7

In the lock-and-key model of enzyme action,the enzyme active site is thought of as ________.

Accepted Answer

A) a rigid,nonflexible shape that fits the substrate exactly 
B) an area of the enzyme that can adjust to fit the substrate shape 
C) a key-like shape that fits into a pocket of the substrate surface 
D) a hydrophilic area on the enzyme surface 
E) a lock that bars a noncompetitive inhibitor from reacting 
A) a rigid,nonflexible shape that fits the substrate exactly 
B) an area of the enzyme that can adjust to fit the substrate shape 
C) a key-like shape that fits into a pocket of the substrate surface 
D) a hydrophilic area on the enzyme surface 
E) a lock that bars a noncompetitive inhibitor from reacting

Question 8

Most enzymes are ________.

Accepted Answer

A) fluid-mosaic proteins 
B) induced proteins 
C) substrate proteins 
D) fibrous proteins 
E) globular proteins 
A) fluid-mosaic proteins 
B) induced proteins 
C) substrate proteins 
D) fibrous proteins 
E) globular proteins

Question 9

Which of the following would be most likely to be deficient in at least one essential amino acid?

Accepted Answer

A) eggs 
B) milk 
C) beans 
D) steak 
E) ham 
A) eggs 
B) milk 
C) beans 
D) steak 
E) ham

Question 10

To what main class of enzymes does the enzyme that catalyzes the conversion of lactose to galactose and glucose belong?

Accepted Answer

A) oxidoreductase 
B) transferase 
C) hydrolase 
D) lyase 
E) isomerase 
A) oxidoreductase 
B) transferase 
C) hydrolase 
D) lyase 
E) isomerase

Question 11

Collagen,a protein found in tendons and cartilage,would be classified as a ________ protein.

Accepted Answer

A) catalytic 
B) structural 
C) transport 
D) storage 
E) hormone 
A) catalytic 
B) structural 
C) transport 
D) storage 
E) hormone

Question 12

An acid can denature a protein by ________.

Accepted Answer

A) agitating the protein chains 
B) disrupting hydrogen bonds between side chains 
C) disrupting hydrophobic interactions within a protein chain 
D) removing helping molecules such as heme 
E) breaking disulfide bridges 
A) agitating the protein chains 
B) disrupting hydrogen bonds between side chains 
C) disrupting hydrophobic interactions within a protein chain 
D) removing helping molecules such as heme 
E) breaking disulfide bridges

Question 13

Amino acids that are not synthesized in the body but must be ingested with the diet are called ________ amino acids.

Accepted Answer

The answer of Amino acids that are not synthesized in...

Question 14

Which of the following functional groups of an amino acid would be in the ionized state at high pH?

Accepted Answer

A)  O  
-C-OH 
B) -   -OH 
C) -   
D)  O  
-C   
E)    
A)  O  
-C-OH 
B) -   -OH 
C) -   
D)  O  
-C   
E)

Question 15

Denaturation of a protein ________.

Accepted Answer

A) changes the primary structure of a protein 
B) disrupts the secondary,tertiary,or quaternary structure of a protein 
C) is always irreversible 
D) hydrolyzes peptide bonds 
E) can only occur in a protein with quaternary structure 
A) changes the primary structure of a protein 
B) disrupts the secondary,tertiary,or quaternary structure of a protein 
C) is always irreversible 
D) hydrolyzes peptide bonds 
E) can only occur in a protein with quaternary structure

Question 16

Which R group would most likely be found in a hydrophobic area of the tertiary structure of a globular protein?

Accepted Answer

A) -   -OH 
B) -   - COO- 
C)    
D) -   -   -   -   -   H3 
E) O -   -   -   
A) -   -OH 
B) -   - COO- 
C)    
D) -   -   -   -   -   H3 
E) O -   -   -

Question 17

Consider the R groups of the following amino acids: cysteine: -   SH; alanine: -   ; serine: -   OH
The name for the dipeptide shown below is ________.   O   OH     H -   - NH   HCOOH

Accepted Answer

A) alanylcysteine 
B) alanylserine 
C) serylalanine 
D) serylcysteine 
E) serinealanine 
A) alanylcysteine 
B) alanylserine 
C) serylalanine 
D) serylcysteine 
E) serinealanine

Question 18

Circle the peptide bond in this structure.

Accepted Answer

The answer of Circle the peptide bond in this structure....

Question 19

Sucrase,the protein that facilitates the hydrolysis of sucrose,would be classified as a ________ protein.

Accepted Answer

A) transport 
B) hormonal 
C) catalytic 
D) structural 
E) contractile 
A) transport 
B) hormonal 
C) catalytic 
D) structural 
E) contractile

Question 20

What type of amino acids has polar side chains that are attracted to water?

Accepted Answer

A) hydrophilic 
B) hydrophobic 
C) nonpolar 
D) aromatic 
E) hydrocarbon 
A) hydrophilic 
B) hydrophobic 
C) nonpolar 
D) aromatic 
E) hydrocarbon

In the peptide Ala-Try-Gly-Phe,the N-terminus is ________.

The optimum pH for the activity of pepsin is about ________.

The presence of enzymes to catalyze bioreactions in our bodies allows ________.

Heat denatures a protein by disrupting ________.

The one letter abbreviation for the amino acid tyrosine is ________.

Hemoglobin has a total of ________ protein chains in its quaternary structure.

In the lock-and-key model of enzyme action,the enzyme active site is thought of as ________.

Most enzymes are ________.

Which of the following would be most likely to be deficient in at least one essential amino acid?

To what main class of enzymes does the enzyme that catalyzes the conversion of lactose to galactose and glucose belong?

Collagen,a protein found in tendons and cartilage,would be classified as a ________ protein.

An acid can denature a protein by ________.

Amino acids that are not synthesized in the body but must be ingested with the diet are called ________ amino acids.

Which of the following functional groups of an amino acid would be in the ionized state at high pH?

Denaturation of a protein ________.

Which R group would most likely be found in a hydrophobic area of the tertiary structure of a globular protein?

Consider the R groups of the following amino acids: cysteine: - SH; alanine: - ; serine: - OH The name for the dipeptide shown below is ________. O OH H - - NH HCOOH

Circle the peptide bond in this structure.

Sucrase,the protein that facilitates the hydrolysis of sucrose,would be classified as a ________ protein.

What type of amino acids has polar side chains that are attracted to water?

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Exam 16: Amino Acids, proteins, and Enzymes

In the peptide Ala-Try-Gly-Phe,the N-terminus is ________.

The optimum pH for the activity of pepsin is about ________.

The presence of enzymes to catalyze bioreactions in our bodies allows ________.

Heat denatures a protein by disrupting ________.

The one letter abbreviation for the amino acid tyrosine is ________.

Hemoglobin has a total of ________ protein chains in its quaternary structure.

In the lock-and-key model of enzyme action,the enzyme active site is thought of as ________.

Most enzymes are ________.

Which of the following would be most likely to be deficient in at least one essential amino acid?

To what main class of enzymes does the enzyme that catalyzes the conversion of lactose to galactose and glucose belong?

Collagen,a protein found in tendons and cartilage,would be classified as a ________ protein.

An acid can denature a protein by ________.

Amino acids that are not synthesized in the body but must be ingested with the diet are called ________ amino acids.

Which of the following functional groups of an amino acid would be in the ionized state at high pH?

Denaturation of a protein ________.

Which R group would most likely be found in a hydrophobic area of the tertiary structure of a globular protein?

Consider the R groups of the following amino acids: cysteine: - SH; alanine: - ; serine: - OH The name for the dipeptide shown below is ________. O OH H - - NH HCOOH

Circle the peptide bond in this structure.

Sucrase,the protein that facilitates the hydrolysis of sucrose,would be classified as a ________ protein.

What type of amino acids has polar side chains that are attracted to water?

Chemistry in Our Lives

Chemistry and Measurement

Matter and Energy

Atoms and Elements

Nuclear Chemistry

Ionic and Molecular Compounds

Chemical Quantities and Reactions

Gases

Solutions

Acids and Bases and Equilibrium

Introduction to Organic Chemistry: Hydrocarbons

Alcohols, thiols, ethers, aldehydes, and Ketones

Carbohydrates

Carboxylic Acids, esters, amines, and Amides

Lipids

Nucleic Acids and Protein Synthesis

Metabolic Pathways and Energy Production

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