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Biochemistry: Proteins

Total questions: 165

Worksheet time: 1hrs 24mins

Name
Class
Date
1.

Which of the following groups are found in every standard amino acid?

a)

Phosphate group and hydroxyl group

b)

Amino group and phosphate group

c)

Amino group and carboxyl group

d)

Hydroxyl group and carboxyl group

2.

What makes glycine unique among the 20 standard amino acids?

a)

It has a ring structure

b)

It lacks a chiral alpha carbon

c)

It is positively charged at physiological pH

d)

It is always phosphorylated in cells

3.

Which amino acid contains a sulfhydryl group capable of forming disulfide bonds?

a)

Tyrosine

b)

Histidine

c)

Serine

d)

Cysteine

4.

What type of bond forms between two amino acids in a protein?

a)

Hydrogen bond

b)

Peptide bond

c)

Disulfide bond

d)

Ionic bond

5.

What is the net result of peptide bond formation between two amino acids?

a)

Addition of a water molecule

b)

A hydrolysis reaction

c)

Elimination of a water molecule (condensation reaction)

d)

Loss of a carbon atom

6.

Which amino acid often introduces bends or kinks in polypeptides due to its rigid ring structure?

a)

Glycine

b)

Proline

c)

Alanine

d)

Serine

7.

How many amino acids make up one full turn of an alpha helix?

a)

3.0

b)

3.8

c)

3.6

d)

4.2

8.

Beta-pleated sheets are primarily stabilized by:

a)

Hydrophobic interactions

b)

Hydrogen bonds between backbone atoms

c)

Ionic bonds between side chains

d)

Peptide bonds

9.

Which amino acid is most commonly found at the centre of collagen’s triple helix?

a)

Proline

b)

Glycine

c)

Cysteine

d)

Tyrosine

10.

What technique did Frederick Sanger use to determine the first protein sequence?

a)

Edman degradation

b)

Mass spectrometry

c)

Gel electrophoresis

d)

NMR

11.

What structure is formed by hydrogen bonding between atoms of the polypeptide backbone?

a)

Secondary structure

b)

Tertiary structure

c)

Quaternary structure

d)

Primary structure

12.

What determines the primary structure of a protein?

a)

Folding of the polypeptide chain

b)

The DNA nucleotide sequence

c)

The R groups of side chains

d)

Post-translational modifications

13.

Which level of protein structure involves interactions between separate polypeptide chains?

a)

Tertiary

b)

Quaternary

c)

Primary

d)

Secondary

14.

What is the typical role of hydrophobic amino acids in protein folding?

a)

They cluster together inside the protein core

b)

They remain on the protein surface

c)

They are phosphorylated

d)

They form ionic bonds

15.

Which experimental technique can resolve atomic structure through electron density maps?

a)

X-ray crystallography

b)

Western blotting

c)

SDS-PAGE

d)

Cryo-EM

16.

What characteristic makes beta sheets particularly strong in fibrous proteins like silk?

a)

Disulfide bonds

b)

Side-chain packing

c)

Extensive hydrogen bonding across sheets

d)

Alpha-helical cores

17.

What type of secondary structure is least favourable for proline residues?

a)

Beta sheets

b)

Alpha helices

c)

Loops

d)

Turns

18.

What structural level is most directly responsible for a protein’s function?

a)

Primary

b)

Secondary

c)

Tertiary

d)

Quaternary

19.

Which domain structure is commonly used to bind DNA or ligands?

a)

Beta strand

b)

Helix-turn-helix motif

c)

Alpha sheet

d)

Disulfide bridge

20.

Which feature defines a protein domain?

a)

Always composed of beta sheets

b)

Always involved in enzymatic reactions

c)

Structurally and functionally independent region

d)

Present only in fibrous proteins

21.

What tool is commonly used to align unknown protein sequences to known homologs?

a)

Chimera

b)

BLAST

c)

Jmol

d)

SDS-PAGE

22.

What is the Ramachandran plot used to show?

a)

DNA mutations

b)

Sequence homology

c)

Allowable dihedral angles in peptide backbones

d)

Molecular weight distribution

23.

Which amino acid is most restricted in its backbone angles?

a)

Glycine

b)

Proline

c)

Serine

d)

Leucine

24.

Which amino acid is least restricted and found throughout the Ramachandran plot?

a)

Glycine

b)

Valine

c)

Isoleucine

d)

Tryptophan

25.

What kind of protein structure is represented by hemoglobin’s tetrameric assembly?

a)

Secondary

b)

Tertiary

c)

Quaternary

d)

Primary

26.

Which technique allows prediction of hydrophobic regions in proteins?

a)

Edman degradation

b)

X-ray crystallography

c)

Hydropathy plots

d)

SDS-PAGE

27.

What is a prosthetic group in a protein?

a)

A sequence of amino acids that determines function

b)

A non-protein component permanently bound to the protein

c)

A protein domain that binds DNA

d)

A weakly bound ligand

28.

What causes the sickle shape in sickle cell anemia?

a)

A single amino acid substitution in hemoglobin

b)

Collagen misfolding

c)

Excessive proline content

d)

Dehydration of red blood cells

29.

Which structural feature of proteins is most conserved during evolution?

a)

DNA sequence

b)

RNA sequence

c)

3D protein fold

d)

Codon usage

30.

Which amino acid often plays a role in enzymatic active sites due to pKa near physiological pH?

a)

Proline

b)

Histidine

c)

Glycine

d)

Valine

31.

What is the main force driving the formation of tertiary protein structure?

a)

Ionic bonds

b)

Disulfide bridges

c)

Hydrophobic interactions

d)

Hydrogen bonding with water

32.

Which tool is used to predict 3D structure from primary sequence using AI?

a)

Chimera

b)

AlphaFold

c)

SDS-PAGE

d)

Edman Tool

33.

What property distinguishes fibrous proteins from globular ones?

a)

Solubility in water

b)

Elongated, structural roles

34.

What is true about globular proteins?

a)

Mostly structural

b)

Compact, often enzymatic or regulatory

c)

Always insoluble

d)

Lack secondary structures

35.

What is the CATH database used for?

a)

Determining DNA sequences

b)

Classifying protein domains by structure

c)

Predicting glycosylation sites

d)

Comparing metabolic rates

36.

Which motif is commonly involved in DNA binding?

a)

Greek key

b)

OB-fold

c)

Helix-turn-helix

d)

Beta-barrel

37.

What happens in a condensation reaction between two amino acids?

a)

Addition of phosphate

b)

Removal of water and formation of peptide bond

c)

Addition of carbon

d)

Removal of a hydrogen atom

38.

Which experimental method is ideal for studying proteins in solution?

a)

X-ray crystallography

b)

NMR spectroscopy

c)

SDS-PAGE

d)

Gel filtration

39.

What structural level describes spatial arrangement of multiple protein subunits?

a)

Tertiary

b)

Quaternary

c)

Secondary

d)

Domain

40.

Which secondary structure contributes most to tensile strength in fibrous proteins?

a)

Alpha-helix

b)

Beta-pleated sheet

c)

Disulfide bridge

d)

Greek key motif

41.

What is the significance of disulfide bonds?

a)

They catalyse metabolic reactions

b)

They stabilise protein folding, especially in extracellular proteins

c)

They link sugars to proteins

d)

They are only found in RNA

42.

What is a ‘missense’ mutation?

a)

A silent change in DNA

b)

A codon change resulting in a different amino acid

c)

A change that introduces a stop codon

d)

Removal of an exon

43.

What defines an ‘antiparallel’ beta sheet?

a)

Amino acids with opposing charges

b)

Adjacent strands run in opposite directions

c)

Alternating alpha helices

d)

Presence of disulfide bonds

44.

How does collagen’s triple helix differ from an alpha helix?

a)

It lacks hydrogen bonding

b)

It contains only polar residues

c)

It has a left-handed triple helix formed from three chains

d)

It is globular and water-soluble

45.

Which amino acid is typically absent from the interior of globular proteins?

a)

Leucine

b)

Aspartic acid

c)

Isoleucine

d)

Phenylalanine

46.

What happens in X-ray crystallography?

a)

NMR is used to detect bond rotation

b)

Crystals diffract X-rays to produce electron density maps

c)

Fluorescence is used to visualise proteins

d)

Antibodies detect the protein

47.

What property allows proteins to separate on SDS-PAGE?

a)

Their charge

b)

Their molecular weight

c)

Their shape

d)

Their isoelectric point

48.

What is the role of the Protein Data Bank (PDB)?

a)

Stores enzyme kinetics data

b)

Archives DNA sequences

c)

Houses experimentally determined protein structures

d)

Calculates protein half-life

49.

What defines a silent mutation?

a)

Changes structure but not function

b)

Alters DNA but not amino acid sequence

c)

Adds a stop codon

d)

Inactivates the gene

50.

What causes antigenic drift in viral proteins?

a)

DNA replication errors

b)

Cell wall synthesis

51.

Which amino acid is most likely to be involved in ionic interactions at physiological pH?

a)

Valine

b)

Glycine

c)

Lysine

d)

Alanine

52.

What does a Ramachandran plot illustrate?

a)

Allowed phi and psi angles in polypeptides

b)

Protein half-lives

c)

Amino acid frequencies

d)

pKa values

53.

Which term best describes the helix-turn-helix?

a)

Supersecondary structure motif

b)

Quaternary fold

c)

Tertiary interaction

d)

Globular domain

54.

What characterizes a beta-alpha-beta motif?

a)

A helix flanked by glycine residues

b)

A central helix between two beta strands

c)

A parallel sheet with alpha helix above

d)

Loop-turn-loop topology

55.

What stabilises beta sheets in protein structures?

a)

Peptide bonds

b)

Hydrogen bonds between backbone atoms

c)

Disulfide bridges

d)

DNA-protein crosslinks

56.

What evolutionary process allows gene families to develop new functions?

a)

Lateral transfer

b)

Gene duplication and divergence

c)

Genetic recombination

d)

RNA editing

57.

What does the term "motif" refer to in protein structure?

a)

Disulfide-linked domains

b)

Unstructured loops

c)

Recurrent folding patterns

d)

Active site residues

58.

Which technique best visualises atomic positions in small proteins in solution?

a)

Western blotting

b)

Edman sequencing

c)

NMR spectroscopy

d)

Mass spectrometry

59.

What makes histidine useful in enzyme active sites?

a)

It can gain or lose a proton at physiological pH

b)

It forms covalent bonds easily

c)

It is extremely rigid

d)

It is always charged

60.

What's the function of BLAST in protein science?

a)

Identifies hydropathy index

b)

Compares protein sequences for similarity

c)

Calculates molecular weight

d)

Measures net charge

61.

In what protein type would you expect a high percentage of proline?

a)

Globular proteins

b)

Collagen

c)

Enzymes

d)

Histones

62.

Which group forms hydrogen bonds in polar uncharged amino acids?

a)

Carbon rings

b)

Side chains containing oxygen or nitrogen

c)

Hydrocarbon tails

d)

Sulfur groups only

63.

Which interaction is least likely to stabilise protein tertiary structure?

a)

Disulfide bonds

b)

Phosphodiester bonds

c)

Hydrophobic interactions

d)

Hydrogen bonds

64.

What is a coenzyme?

a)

Protein structure that forms sheets

b)

An enzyme regulator

c)

A loosely bound organic cofactor

d)

An unfolded domain

65.

What distinguishes quaternary structure from tertiary?

a)

Number of alpha helices

b)

Involves interactions between polypeptide chains

c)

Includes only disulfide bridges

d)

Is determined solely by RNA

66.

Which residue introduces flexibility into protein structure?

a)

Proline

b)

Glycine

c)

Cysteine

d)

Arginine

67.

Which of the following proteins does NOT typically have quaternary structure?

a)

Myoglobin

b)

Collagen

68.

What do Greek key motifs consist of?

a)

Alternating helices

b)

Four beta strands folded into a pattern

c)

Random coil structures

d)

Zinc-finger repeats

69.

Which experimental technique requires protein crystallisation?

a)

X-ray crystallography

b)

SDS-PAGE

c)

Cryo-EM

d)

Northern blotting

70.

What effect does the substitution of a hydrophobic residue with a polar one often have?

a)

Increases solubility

b)

Alters protein folding or function

c)

Enhances stability

d)

Prevents translation

71.

What is the “central dogma” of biology?

a)

DNA → carbohydrate → ATP

b)

DNA → RNA → Protein

c)

RNA → DNA → Protein

d)

Protein → DNA → RNA

72.

Which type of beta sheet is more stable?

a)

Parallel

b)

Antiparallel

c)

Right-handed

d)

Alpha-loop

73.

Which structural level is directly affected by a mutation in the gene coding sequence?

a)

Primary structure

b)

Tertiary structure

c)

Quaternary structure

d)

Secondary motif

74.

Why are Ramachandran plots important in structure validation?

a)

They show which bond angles are sterically allowed

b)

They predict disulfide bonds

c)

They visualise hydrophobic domains

d)

They measure isoelectric points

75.

What is true about collagen?

a)

It forms a tetrameric globular structure

b)

It consists of three polypeptides in a triple helix

c)

It’s soluble in cytoplasm

d)

It lacks secondary structure

76.

What is a characteristic of proteins with high structural conservation but low sequence similarity?

a)

They often have similar functions despite differing amino acid sequences

b)

They lack tertiary structure

c)

They cannot be identified by BLAST

d)

They do not fold into domains

77.

Which of the following is NOT a type of protein post-translational modification?

a)

Phosphorylation

b)

Translation

c)

Ubiquitination

d)

Acetylation

78.

What determines the 3D shape of a protein?

a)

Length of the polypeptide

b)

Amino acid sequence and side chain interactions

c)

mRNA folding

d)

Protein degradation

79.

Why are hydrophobic residues usually buried inside the protein core?

a)

They are too large to be on the surface

b)

They are excluded from aqueous environments

c)

They are acidic

d)

They form hydrogen bonds

80.

What term describes a segment of a protein that folds independently and performs a specific function?

a)

Motif

b)

Domain

c)

Subunit

d)

Codon

81.

What is the purpose of SDS in SDS-PAGE?

a)

To denature proteins and impart uniform negative charge

b)

To stain proteins

c)

To buffer the gel

d)

To increase pH

82.

What part of an amino acid determines its chemical characteristics?

a)

Carboxyl group

b)

R group (side chain)

c)

Amino group

d)

Peptide bond

83.

Which of the following best defines antigenic drift?

a)

Sudden genetic recombination in viruses

b)

Transfer of DNA between species

c)

Accumulation of amino acid changes in viral surface proteins

d)

Viral particle degradation

84.

Which amino acid is classified as non-polar and hydrophobic?

a)

Aspartate

b)

Glutamine

c)

Leucine

d)

Serine

85.

What amino acid is often found in active sites and has an imidazole side chain?

a)

Proline

b)

Alanine

c)

Histidine

d)

Cysteine

86.

What defines a synonymous mutation?

a)

A frameshift

b)

A nucleotide change that does not alter the amino acid

c)

A mutation in the promoter region

d)

A change that stops transcription

87.

What makes proline unique among amino acids?

a)

It's aromatic

b)

It has a negative charge

c)

It forms a ring with the backbone, restricting flexibility

d)

It cannot form peptide bonds

88.

What term describes proteins made of more than one polypeptide chain?

a)

Homologs

b)

Monomers

c)

Multimeric proteins

d)

Globulins

89.

Which protein classification describes proteins like myoglobin and enzymes?

a)

Fibrous

b)

Globular

c)

Disordered

d)

Crystallised

90.

In an alpha helix, which atoms form the hydrogen bond stabilizing the structure?

a)

R groups

b)

Backbone amide hydrogen and carbonyl oxygen

c)

Side-chain carbon and nitrogen

d)

Sulfur and phosphate

91.

Which tool would you use to visualise protein 3D structures?

a)

BLAST

b)

PyMOL

c)

SDS-PAGE

d)

UniProt

92.

What is a key feature of fibrous proteins like keratin or collagen?

a)

Compact tertiary structures

b)

Extended, rope-like structures

93.

What is the first step in Edman degradation?

a)

Protein hydrolysis

b)

Cleaving the N-terminal amino acid

c)

Labeling the C-terminal

d)

Denaturation

94.

Why is protein crystallisation a limitation for X-ray studies?

a)

It requires radioactive isotopes

b)

Not all proteins form crystals

c)

It destroys protein function

d)

It only works for enzymes

95.

What happens when a charged amino acid is substituted for a hydrophobic one?

a)

It forms a disulfide bond

b)

It can disrupt protein structure and function

c)

It increases crystallisation

d)

It always improves binding

96.

Which of these is NOT typically used for protein structure prediction?

a)

AlphaFold

b)

Southern blotting

c)

Hydropathy plots

d)

BLAST

97.

What does UniProt provide?

a)

Protein crystallisation kits

b)

Functional and sequence information on proteins

c)

DNA sequencing software

d)

Ramachandran plots

98.

Which term refers to genes in different species that evolved from a common ancestor?

a)

Paralogs

b)

Orthologs

c)

Isomers

d)

Isozymes

99.

Which of the following is NOT a characteristic of cysteine?

a)

Contains sulfur

b)

Forms disulfide bridges

c)

Has a methyl side chain

d)

Participates in catalytic activity

100.

What causes the flexibility of polypeptide turns and loops?

a)

Disulfide bonds

b)

High proline content

c)

Glycine residues and lack of regular structure

d)

Charged residues

101.

Zwitterion form of amino acid is  …………

a)

Nonionic form

b)

Dipolar form 

c)

Molecular form

d)

Charged form

102.

Globular proteins are  …………

a)

Insoluble in water

b)

Extended along one axis

c)

Spherical in shape

d)

Thread like structures

103.

Alpha keratin is not present in …………….

a)

Hair

b)

Nail    

c)

Horns

d)

Bones

104.

Amino acid behaves as 

a)

Proton donar 

b)

Proton acceptor

c)

Ampholyte     

d)

Salt

105.

Beta pleated sheet structure is a ……………. structure

(a)  

106.

Amino acids contain how many functional groups?

4 lines
107.

Draw the structure of alpha amino acids

108.

Semipermeable membrane is used in

4 lines
109.

Which of the following is a transport protein

a)

Casein

b)

Hemoglobin 

c)

Collagen

d)

Fibroin

110.

Amino acid containing –SH group is

a)

Serine

b)

Cystein

c)

Glycine

d)

Methionine

111.

All proteins contain the

a)

Same 20 amino acids

b)

Different amino acids

c)

300 Amino acids occurring in nature

d)

Only a few amino acids

112.

The optically inactive amino acid is

a)

Glycine

b)

Serine

c)

Threonine

d)

Valine

113.

Sulphur containing amino acid is

a)

Methionine

b)

Leucine

c)

Valine

d)

Asparagine

114.

An example of sulphur containing amino acid is

a)

2-Amino-3-mercaptopropanoic acid

b)

2-Amino-3-methylbutanoic acid

c)

2-Amino-3-hydroxypropanoic acid

d)

Amino acetic acid

115.

All the following are sulphur containing amino acids found in proteins except

a)

Cysteine

b)

Cystine

c)

Methionine

d)

Threonine

116.

An aromatic amino acid is

a)

Lysine

b)

Tyrosine

c)

Taurine

d)

Arginine

117.

Amino acid with side chain containing basic groups is

a)

2-Amino 5-guanidovaleric acid

b)

2-Pyrrolidine carboxylic acid

c)

2-Amino 3-mercaptopropanoic acid

d)

2-Amino propanoic acid

118.

An essential amino acid in man is

a)

Aspartate

b)

Tyrosine

c)

Methionine

d)

Serine

119.

Non essential amino acids

a)

Are not components of tissue proteins

b)

May be synthesized in the body from essential

amino acids

c)

Have no role in the metabolism

d)

May be synthesized in the body in diseased

states

120.

Which one of the following is semiessential amino acid for humans?

a)

Valine

b)

Arginine

c)

Lysine

d)

Tyrosine

121.

The amino acid with a nonpolar side chain is

a)

Serine

b)

Valine

c)

Asparagine

d)

Threonine

122.

Biuret reaction is specific for

a)

–CONH-linkages

b)

–CSNH2 group

c)

–(NH)NH2 group

d)

All of these

123.

Sakaguchi’s reaction is specific for

a)

Tyrosine

b)

Proline

c)

Arginine

d)

Cysteine

124.

Million-Nasse’s reaction is specific for the amino acid:

a)

Tryptophan

b)

Tyrosine

c)

Phenylalanine

d)

Arginine

125.

In proteins the α-helix and β-pleated sheet are examples of

a)

Primary structure

b)

Secondary structure

c)

Tertiary structure

d)

Quaternary structure

126.

At the lowest energy level α-helix of polypeptide chain is stabilised

a)

By hydrogen bonds formed between the H of

peptide N and the carbonyl O of the residue

b)

Disulphide bonds

c)

Non polar bonds

d)

Ester bonds

127.

The a-helix of proteins is

a)

A pleated structure

b)

Made periodic by disulphide bridges

c)

A non-periodic structure

d)

Stabilised by hydrogen bonds between NH

and CO groups of the main chain

128.

Denaturation of proteins results in

a)

Disruption of primary structure

b)

Breakdown of peptide bonds

c)

Destruction of hydrogen bonds

d)

Irreversible changes in the molecule

129.

Proteins contain

a)

Only L- α- amino acids

b)

Only D-amino acids

c)

DL-Amino acids

d)

Both (A) and (B)

130.

At neutral pH, a mixture of amino acids in solution would be predominantly:

a)

Dipolar ions

b)

Nonpolar molecules

c)

Positive and monovalent

d)

Hydrophobic

131.

The monomer making up a polypeptide chain.

a)

glucose

b)

amino acid

c)

protein

d)

DNA

132.

In this image what does R represent

a)

an element

b)

a carbon atom

c)

a functional group

d)

a carboxyl group

133.

Which level of protein structure is shown here?

a)

tertiary structure

b)

secondary structure

c)

quaternary structure

d)

primary structure

134.

How would you describe the bonds shown in this diagram?

a)

strong covalent bonds

b)

ionic bonds

c)

non-polar interactions

d)

hydrogen bonds

135.

Which level of protein structure is shown here?

a)

tertiary structure

b)

secondary structure

c)

quaternary structure

d)

primary structure

136.

How would you describe the bonds indicated in this diagram?

a)

strong covalent bonds

b)

ionic bonds

c)

non-polar interactions

d)

hydrogen bonds

137.

Which levels of protein structure are shown here?

a)

primary structure

b)

tertiary structure

c)

primary and secondary structure

d)

quaternary structure

138.

Which side groups can form hydrogen bonds?

a)

-COOH

b)

-CH

c)

-HS

d)

-CH3

139.

Which statement is NOT true of this collagen molecule?

a)

it is insoluble

b)

it contains just a few types of amino acid

c)

it is a globular protein

d)

it is a strong molecule

140.

Which statement is NOT true of this haemoglobin molecule?

a)

it has tertiary structure

b)

it is a fibrous protein

c)

it is soluble

d)

it has quaternary structure

141.

Enzymes are proteins. Which phrase best describes the function of enzymes?

a)

They take part in biochemical reactions

b)

They make reactions happen in the body

c)

They speed up biochemical reactions by lowering the activation energy

d)

They are catalysts

142.

Which phrase best explains the increase in rate between 10oC and 30oC?

a)

Enzymes and substrates collide more often

b)

The enzyme is working faster

c)

The temperature is increasing

d)

The rate of reaction is increasing

143.

Which phrase best explains the low rate at 50oC?

a)

The enzyme is not at its optimum temperature

b)

The substrate has melted

c)

The enzyme has denatured

d)

The temperature is too high

144.

All enzymes have an optimum temperature of 37oC.

a)

True

b)

False

145.

All enzymes are most effective at pH 7

a)

True

b)

False

146.

Which of the following are true of the secondary structure of proteins? Select all that apply!

a)

One formation is the beta helix

b)

One formation is the alpha helix

c)

They are stabilized by hydrogen bonds

d)

One formation is the beta-pleated sheet

e)

They are stabilized by peptide bonds

147.

Which of the following are a component of amino acids? Select all that apply!

a)

Central calcium atom

b)

Carboxyl group

c)

Phosphate group

d)

Amino group

e)

Central carbon atom

148.

What is the monomer of a protein?

a)

Amino acid

b)

Phospholipid

c)

Nucleotide

d)

Simple sugars

149.

Describe the side-chain of this amino acid.

a)

Non-polar and hydrophobic

b)

Polar and uncharged

c)

Polar and charged (basic)

d)

Polar and charged (acidic)

150.

Describe the side-chain of this amino acid.

a)

Non-polar and hydrophobic

b)

Polar and uncharged

c)

Polar and charged (basic)

d)

Polar and charged (acidic)

151.

A ___________ is a covalent bond that forms between two ___________ amino acids.

a)

Peptide ; cysteine

b)

Hydrophobic effect ; nonpolar

c)

Hydrophilic effect ; polar

d)

Disulfide bridge; cysteine

e)

Disulfide bridge ; serine

152.

Proteins are formed via ________ reactions, in which water is a _______.

a)

dehydration; reactant

b)

dehydration; product

c)

hydrolysis; reactant

d)

hydrolysis; product

153.

Which of the following are true of R-groups, or sidechains, on amino acids? Select all that apply.

a)

They give amino acids their identity

b)

They may be charged or uncharged

c)

They may be hydrophobic or hydrophilic

d)

They are identical across all amino acids

e)

They form peptide bonds with other R-groups

154.

Which interaction forms between nonpolar R-groups?

a)

Hydrogen bonds

b)

Peptide bonds

c)

Disulfide bridges

d)

Hydrophobic effects

e)

Ionic bonds

155.

To build a polypeptide, amino acids form __________ bonds, which are _________.

a)

Hydrogen ; weak

b)

Hydrogen ; strong

c)

Peptide ; covalent

d)

Peptide ; ionic

e)

Ionic ; strong

156.
What is a protein: 
a)
A polymer composed of many sugars.
b)
A polymer composed of many amino acids. 
c)
A polymer composed of fatty acids. 
d)
A polymer composed of nucleotides. 
157.
How many different amino acids are there?
a)
15
b)
20
c)
25
d)
30
158.
The diagram shows a bond forming between two amino acids. What is the name of this reaction?
a)
Dehydration Synthesis
b)
Hydrolysis
c)
Pepysis
d)
Oxidation
159.
What is a peptide bond?
a)
Bond that holds two amino acids together.
b)
A bond that holds hydrogen and oxygen molecules together.
c)
A bond that holds the phosphate group of one nucleotide and a sugar of a neighboring nucleotide.
d)
A bond that is formed by the sharing of electrons.
160.
Each amino acid is different from the other due to....
a)
The R group
b)
The amino group
c)
The carboxyl group
d)
The central carbon
161.

What happens in this process?

a)

Speed up chemical reactions

b)

Control cell growth

c)

Involved in body structure.

d)
Single Displacement
162.
What is the monomer of a protein?
a)
amino acid
b)
monosaccharide
c)
fatty acid
d)
nucleic acid
163.

The entire polypeptide forms a three-dimensional structure

a)

Primary

b)

Secondary

c)

Tertiary

d)

Quaternary

164.

Any type of three-dimensional structure of proteins?

a)

Primary

b)

Secondary (pleat)

c)

Secondary (Helix)

d)

Quaternary

165.

What is low in protein?

a)

Egg

b)

meat and fish

c)

fruits and vegetables

d)

seeds and nuts

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