Characteristics of Proteins: Return To TOC

Section 20.
Characteristics of Proteins
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Copyright ©2016 Cengage Learning. All Rights Reserved. 1

Chapter 20
Chapter Outline
20.1Characteristics of proteins
20.2Amino acids: The building blocks for proteins
20.3Essential amino acids
20.4Chirality and amino acids
20.5Acid–base properties of amino acids
20.6Cysteine: A chemically unique amino acid
20.7Peptides
20.8Biochemically important small peptides
20.9General structural characteristics of proteins
20.10 Primary structure of proteins

Chapter 20
Chapter Outline
20.11Secondary structure of proteins

20.12Tertiary structure of proteins
20.13Quaternary structure of proteins
20.14Protein hydrolysis
20.15Protein denaturation
20.16Protein classification based on shape
20.17Protein classification based on function
20.18Glycoproteins
20.19Lipoproteins

Section 20.1
• Protein: Naturally-occurring, unbranched

polymer in which the monomer units are amino
acids
• Most abundant substance in cells after water
– Account for about 15% of a cell’s overall mass
• Elemental composition - Carbon (C), hydrogen
(H), nitrogen (N), oxygen (O), and sulfur (S)
– Average nitrogen content is 15.4% by mass
• Contain iron (Fe), phosphorus (P), and other
metals in certain specialized proteins
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Section 20.1
Proteins are naturally occurring polymers in which

the monomer units are _____.
a.triacylglycerols
b.amino acids
c.carbohydrates
d.nucleosides
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Section 20.1
Proteins are naturally occurring polymers in which

the monomer units are _____.
a.triacylglycerols
b.amino acids
c.carbohydrates
d.nucleosides
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Section 20.2
Amino Acids: The Building Blocks for Proteins
Amino Acids
• Contain both an amino (—NH2) and a carboxyl

(—COOH) group
– -amino acids: Amino acids in which the amino
group and the carboxyl group are attached to the -
carbon atom
• Side chains (R) - Vary in size, shape, charge, acidity,
functional groups present, hydrogen-bonding ability,
and chemical reactivity
– >700 amino acids are known
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Section 20.2
Standard Amino Acids

• 20 -amino acids normally found in proteins
• Divided based on the properties of R-groups
– Nonpolar amino acids: Contain one amino group,
one carboxyl group, and a nonpolar side chain
• Hydrophobic - Not attracted to water molecules
• Found in the interior of proteins, where there is no
polarity
– Polar amino acids - Hydrophilic
• Types - Polar neutral, polar acidic, and polar basic
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Section 20.2
Polar Amino Acids

• Polar neutral: Contain polar but neutral side
chains
– Six amino acids belong to this category
• Polar acidic: Contain a carboxyl group as part
of the side chains
– Two amino acids belong to this category
• Polar basic: Contain an amino group as part of
the side chain
– Three amino acids belong to this category
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Section 20.2
Nomenclature
• Three-letter abbreviations are used for naming
standard amino acids
– Abbreviations are the first three letters of the amino
acid’s name
• Exceptions: Isoleucine (Ile), tryptophan (Trp),
asparagine (Asn), and glutamine (Gln)
– One-letter symbols - Used for comparing amino acid
sequences of proteins
• Usually the first letter of the name
• When more than one amino acid has the same letter,
the most abundant amino acid gets the 1st letter
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Section 20.2
Table 20.1 - 20 Standard Amino Acids
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Section 20.2
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Section 20.2
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Section 20.2
Practice Exercise
• Classify the following amino acids based on the
polarity of their R-groups.
O
O
d. H 2N CH C OH
a. H 2N CH C OH
CH2
CH3
O
H 2N CH C OH
CH2
b.
O
H 2N CH C OH
e. CH2
OH
CH2
CH2
O CH2
c. H 2N CH C OH NH2
CH2
C O
OH
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Section 20.2
Practice Exercise
• Classify the following amino acids based on the
polarity of their R-groups.
O
O
d. H 2N CH C OH
a. H 2N CH C OH
CH2
CH3
Non-polar
O
Non-polar
H 2N CH C OH
CH2
b.
O
H 2N CH C OH
e. CH2
Polar Neutral OH
CH2
CH2
O CH2
c. H 2N CH C OH NH2 Polar Basic
CH2
Polar Acidic C O
OH
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Section 20.2
Amino acids are organic compounds that contain a

_____ group and a _____ group and are found in
proteins as _____.
a.hydroxy; carboxyl; -hydroxy amino acids

b.amino; carboxyl; -amino acids
c.amino; carboxyl; beta amino acids
d.hydroxy; carboxyl; beta hydroxy amino acids
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Section 20.2
Amino acids are organic compounds that contain a

_____ group and a _____ group and are found in
proteins as _____.
a.hydroxy; carboxyl; -hydroxy amino acids

b.amino; carboxyl; -amino acids
c.amino; carboxyl; beta amino acids
d.hydroxy; carboxyl; beta hydroxy amino acids
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Section 20.3
Essential Amino Acids
• Standard amino acids needed for protein

synthesis and must be obtained from dietary
sources
– Types of dietary proteins - Complete, incomplete,
and complementary
Arginine* Methionine
Histidine Phenylalanine
*Not essential for adults but is required for growth in
Isoleucine Threonine children
Leucine Tryptophan
Lysine Valine
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Section 20.3
Incomplete dietary proteins contain inadequate

amounts of:
a.one or more essential amino acids.

b.one or more nonessential amino acids.
c.at least one essential and one nonessential amino acid.
d.none of the above.
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Section 20.3
Incomplete dietary proteins contain inadequate

amounts of:
a.one or more essential amino acids.

b.one or more nonessential amino acids.
c.at least one essential and one nonessential amino acid.
d.none of the above.
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Section 20.4
Chirality and Amino Acids
• Four different groups are attached to the -

carbon atom in all of the standard amino acids
– Exception: In glycine, the R-group is hydrogen
• 19 of the 20 standard amino acids contain a
chiral center
– Molecules with chiral centers exhibit enantiomerism
(left- and right-handed forms)
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Section 20.4
• Amino acids found in nature and in proteins are

ʟ isomers
– Exceptions: Some bacteria
– Monosaccharides prefer ᴅ isomers
• Rules for drawing Fischer projection formulas for
amino acid structures
– —COOH group is placed at the top of the projection
formula
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Section 20.4
– R group is placed at the

bottom, positions the carbon
chain vertically
– —NH2 group is placed in a
horizontal position
– NH2 on the left - ʟ
isomer
– NH2 on the right - ᴅ
isomer
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Section 20.4
Practice Exercise
• Name the following amino acids with correct designation for the enantiomer (chiral
carbon is indicated by *).
A B C
COOH COOH COOH
*C *C H 2N *C H
H2N H H NH2
CH CH3 CH 2 CH 2
CH2 SH
CH3
OH
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Section 20.4
Practice Exercise
• Name the following amino acids with correct designation for the enantiomer (chiral
carbon is indicated by *).
A B C
COOH COOH COOH
*C *C H 2N *C H
H2N H H NH2
CH CH3 CH 2 CH 2
CH2 SH
CH3
A = L-isoleucine OH
B = D-cysteine
C = L-tyrosine
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Section 20.4
With few exceptions, the amino acids found in

nature and in proteins are _____ isomers.
a.alpha
b.beta
c.ᴅ
d.ʟ
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Section 20.4
With few exceptions, the amino acids found in

nature and in proteins are _____ isomers.
a.alpha
b.beta
c.ᴅ
d.ʟ
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Section 20.5
Acid–Base Properties of Amino Acids
• In pure form, amino acids are white crystalline

solids
– Decompose before they melt
• Not very soluble in water
• -amino acids exist as zwitterions in solution
and in solid state
– Zwitterions: Molecules with positive charge on one
atom and negative charge on another, but have no
net charge
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Section 20.5
• Carboxyl groups give up protons to produce a

negatively charged species
• Amino groups accept protons to produce a positively
charged species
• Amino acid forms in solution
– Zwitterions, positive ion, and negative ion
– Equilibrium shifts with change in pH
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Section 20.5
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Section 20.5
Isoelectric Point (pI)
• pH at which an amino acid exists in its zwitterion

form
– Carries zero net charge
• Different amino acids have different isoelectric
points
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Section 20.5
An amino acid with a positive charge on one atom

and a negative charge on another atom with an
overall charge of zero is known as a _____.
a.zeroion
b.zwitterion
c.neutral ion
d.neutron
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Section 20.5
An amino acid with a positive charge on one atom

and a negative charge on another atom with an
overall charge of zero is known as a _____.
a.zeroion
b.zwitterion
c.neutral ion
d.neutron
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Section 20.6
Cysteine: A Chemically Unique Amino Acid
• Standard amino acid that has a side chain that

contains a sulfhydryl group (—SH group)
– Sulfhydryl group imparts cysteine a unique chemical
property
• Cysteine, in the presence of mild oxidizing
agents, dimerizes to form a cystine molecule
– Cystine contains two cysteine residues linked via a
covalent disulfide bond
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Section 20.6
What functional group in the amino acid cysteine

gives it the ability to react with another cysteine to
form a cystine molecule?
a.Amino group
b.Carboxyl group
c.Sulfhydryl group
d.Hydroxyl group
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Section 20.6
What functional group in the amino acid cysteine

gives it the ability to react with another cysteine to
form a cystine molecule?
a.Amino group
b.Carboxyl group
c.Sulfhydryl group
d.Hydroxyl group
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Section 20.7
Peptides
Nature of the Peptide Bond
• Under proper conditions, amino acids can bond

together to produce a peptide chain
– Peptide: Unbranched chain of amino acids
• Dipeptide - Compound containing two amino acids
• Oligopeptide - Peptide with 10 to 20 amino acid
residues
• Polypeptide: Long unbranched chain of amino acids
– Reaction is between the amino group of one amino
acid and the carboxyl group of another amino acid
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Section 20.7
Peptides
Nature of the Peptide Bond

• Length of the amino acid chain can vary from a
few amino acids to hundreds of amino acids
– Peptide bonds: Covalent bonds between amino
acids in a peptide
• Every peptide has an N-terminal end and a C-
terminal end
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Section 20.7
Peptides
Peptide Nomenclature
• C-terminal amino acid residue keeps its full
amino acid name
• All of the other amino acid residues have names
that end in -yl
– -yl suffix replaces the -ine or -ic acid ending of the
amino acid name, except for tryptophan, for which -yl
is added to the name
• Amino acid naming sequence begins at the N-
terminal amino acid residue
• Example: Ala-leu-gly has the IUPAC name of
alanylleucylglycine Return to TOC

Section 20.7
Peptides
Isomeric Peptides
• Peptides that contain the same amino acids but
present in different order are different molecules
(constitutional isomers) with different properties
– For example, two different dipeptides can be formed
from one molecule of alanine and glycine
• Number of possible isomeric peptides increases
rapidly as the length of the peptide chain
increases
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Section 20.7
Peptides
How many isomeric peptides are possible from a

peptide of four different amino acids?
a.8
b.12
c.16
d.24
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Section 20.7
Peptides
How many isomeric peptides are possible from a

peptide of four different amino acids?
a.8
b.12
c.16
d.24
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Section 20.8
Biochemically Important Small Peptides
Small Peptide Hormones

• Best-known peptide hormones - Oxytocin and
vasopressin
– Produced by the pituitary gland
– Hormones are nonapeptides (nine amino acid
residues)
• Have six of the residues held in the form of a loop by a
disulfide bond formed from the interaction of two
cysteine residues
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Section 20.8
Small Peptide Neurotransmitters

• Enkephalins are pentapeptide neurotransmitters
produced by the brain
– Bind receptor sites in the brain to reduce pain
• Best-known enkephalins
– Met-enkephalin: Tyr–Gly–Gly–Phe–Met
– Leu-enkephalin: Tyr–Gly–Gly–Phe–Leu
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Section 20.8
Small Peptide Antioxidant

• Glutathione (Glu–Cys–Gly) - Tripeptide present in
high levels in most cells
– Regulates oxidation–reduction reactions
– Antioxidant that protects cellular contents from
oxidizing agents such as peroxides and superoxides
– Unusual structural feature - Glu is bonded to Cys
through the side-chain carboxyl group
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Section 20.8
What small peptides are produced in the brain to

reduce pain, and which play a role in the “high”
reported by long-distance runners?
a.Oxytocin
b.Vasopressin
c.Enkephalins
d.Glutathione
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Section 20.8
What small peptides are produced in the brain to

reduce pain, and which play a role in the “high”
reported by long-distance runners?
a.Oxytocin
b.Vasopressin
c.Enkephalins
d.Glutathione
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Section 20.9
General Structural Characteristics of Proteins
Protein
• General definition - Naturally-occurring,
unbranched polymer in which the monomer units
are amino acids
• Specific definition - Peptide in which at least 40
amino acid residues are present
– The terms polypeptide and protein are used
interchangeably to describe a protein
– Several proteins have >10,000 amino acid residues
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Section 20.9
Protein
– Common proteins contain 400–500 amino acid
residues
– Small proteins contain 40–100 amino acid residues
• More than one polypeptide chain may be
present in a protein
– Monomeric: Protein which contains one polypeptide
chain
– Multimeric: Protein which contains two or more
polypeptide chains
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Section 20.9
Protein Classification Based on Chemical Composition

• Simple protein: Protein in which only amino
acid residues are present
– More than one protein subunit may be present
• Conjugated protein: Protein that has one or
more non-amino-acid entities (prosthetic
groups) present in its structure
– One or more polypeptide chains may be present
– Non-amino-acid components may be organic or
inorganic
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Section 20.9
Protein Classification Based on Chemical Composition

– May be classified further based on the nature of
prosthetic group(s) present
• Lipoprotein contains lipid prosthetic groups
• Glycoprotein contains carbohydrate groups
• Metalloprotein contains a specific metal as its
prosthetic group
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Section 20.9
A _____ protein contains only amino acid residues,

and a _____ protein contains one or more non-
amino acids in the structures.
a.simple; conjugated
b.simple; prosthetic
c.conjugated; simple
d.conjugated; prosthetic
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Section 20.9
A _____ protein contains only amino acid residues,

and a _____ protein contains one or more non-
amino acids in the structures.
a.simple; conjugated
b.simple; prosthetic
c.conjugated; simple
d.conjugated; prosthetic
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Section 20.10
Primary Structure of Proteins
• Types of structures - Primary, secondary,

tertiary, and quaternary
• Primary structure: Order in which amino acids
are linked together in a protein
• Every protein has its own unique amino acid
sequence
– Frederick Sanger sequenced and determined the
primary structure for the first protein (insulin) in 1953
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Section 20.10
Figure 20.4 - Primary

Structure of a Human
Myoglobin
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Section 20.10
• Primary structure of a specific protein is the

same within the organism
– Structures of certain proteins are similar among
different species of animals
• Example: Insulin from pigs, cows, sheep, and humans
are similar but not identical
• Amino acids are linked to each other by peptide
linkages
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Section 20.10
Differences in Animal and Human Insulin
• Immunological reactions gradually increase over

time because animal insulin is foreign to the
human body
• Human insulin produced from genetically
engineered bacteria is available
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Section 20.10
Important Points Regarding Peptide Bond Geometry

• Peptide linkages are essentially planar
– For two amino acids linked through a peptide bond,
six atoms lie in the same plane
– Planar peptide linkage structure has considerable
rigidity, therefore rotation of groups about the C—N
bond is hindered
• Cis–trans isomerism is possible about C—N bond
• Trans isomer is the preferred orientation
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Section 20.10
The order in which amino acids are linked in a

protein is known as the _____ structure.
a.primary
b.secondary
c.tertiary
d.quaternary
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Section 20.10
The order in which amino acids are linked in a

protein is known as the _____ structure.
a.primary
b.secondary
c.tertiary
d.quaternary
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Section 20.11
Secondary Structure of Proteins
• Arrangement in space adopted by the backbone

portion of a protein
• Types - Alpha-helix ( helix) and the beta-
pleated sheet ( pleated sheet)
• Alpha-helix structure: A single protein chain
adopts a shape that resembles a coiled spring
(helix)
– Coil configuration maintained by hydrogen bonds
– Twist of the helix forms a right-handed, or clockwise,
spiral
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Section 20.11
– Hydrogen bonds
between C=O and N
—H entities are
orientated parallel to
the axis of the helix
– All of the amino acid
R groups extend
outward from the
spiral
• There is not enough
room within the
spiral
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Section 20.11
• Beta-pleated sheet structure: Two fully

extended protein chain segments in the same or
different molecules
– Held together by hydrogen bonds
• H-bonding between chains - Inter and/or intramolecular
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Section 20.11
The two most common types of secondary

structures of proteins are the _____ and the
_____.
a.alpha helix; alpha pleated sheet

b.beta helix; alpha pleated sheet
c.alpha helix; beta pleated sheet
d.beta helix; beta pleated sheet
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Section 20.11
The two most common types of secondary

structures of proteins are the _____ and the
_____.
a.alpha helix; alpha pleated sheet

b.beta helix; alpha pleated sheet
c.alpha helix; beta pleated sheet
d.beta helix; beta pleated sheet
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Section 20.12
Tertiary Structure of Proteins
• Overall three-dimensional shape of a protein

• Results from the interactions between amino
acid side chains (R groups) that are widely
separated from each other
• Types of stabilizing interactions observed
– Covalent disulfide bonds
– Electrostatic attractions (salt bridges)
– Hydrogen bonds
– Hydrophobic attractions
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Section 20.12
Types of Stabilizing Interactions

• Disulfide bonds - Covalent, strong, and involve
two cysteine units
• Electrostatic interactions (salt bridges) - Involve
the interaction between charged side chains of
acidic and basic amino acids
• Hydrogen bonds - Can occur between amino
acids with polar R groups
• Hydrophobic interactions - Occur when two
nonpolar side chains are close to each other
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Section 20.12
Figure 20.13 - Stabilizing Influences that Contribute to

the Tertiary Structure
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Section 20.12
What type of attractive interaction, that contributes

to the tertiary structure of a protein, would be
found buried in a nonaqueous environment within
the protein?
a.Hydrogen bonds
b.Salt bridges
c.Hydrophilic interactions
d.Hydrophobic interactions
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Section 20.12
What type of attractive interaction, that contributes

to the tertiary structure of a protein, would be
found buried in a nonaqueous environment within
the protein?
a.Hydrogen bonds
b.Salt bridges
c.Hydrophilic interactions
d.Hydrophobic interactions
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Section 20.13
Quaternary Structure of Proteins
• Organization among the various peptide

subunits in a multimeric protein
– Highest level of protein organization
– Found in proteins that have two or more polypeptide
chains (subunits)
– Subunits are independent of each other and not
covalently bonded to each other
– Contain even number of subunits
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Section 20.13
The structure of hemoglobin, with organization of

its alpha and beta subunits, is an example of what
type of protein structure?
a.Primary
b.Secondary
c.Tertiary
d.Quaternary
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Section 20.13
The structure of hemoglobin, with organization of

its alpha and beta subunits, is an example of what
type of protein structure?
a.Primary
b.Secondary
c.Tertiary
d.Quaternary
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Section 20.14
Protein Hydrolysis
• Reverse of peptide bond formation

– Results in the regeneration of an amine and
carboxylic acid functional groups
– Protein digestion - Enzyme-catalyzed hydrolysis
• Free amino acids produced are absorbed into the
bloodstream and transported to the liver for the
synthesis of new proteins
– Hydrolysis of cellular proteins to amino acids is an
ongoing process, as the body resynthesizes needed
molecules and tissue
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Section 20.14
Protein Hydrolysis
Which of the following best describes what

happens to a small peptide when placed in an acid
solution and heated?
a.The small peptide combines to form a long-chain protein.
b.The small peptide is resistant to acid and heat.
c.The small peptide undergoes hydrolysis to produce free
amino acids.
d.The small peptide undergoes hydrolysis to produce free
amino acids, which recombine upon cooling to form a
different peptide.
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Section 20.14
Protein Hydrolysis
Which of the following best describes what

happens to a small peptide when placed in an acid
solution and heated?
a.The small peptide combines to form a long-chain protein.
b.The small peptide is resistant to acid and heat.
c.The small peptide undergoes hydrolysis to produce free
amino acids.
d.The small peptide undergoes hydrolysis to produce free
amino acids, which recombine upon cooling to form a
different peptide.
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Section 20.15
Protein Denaturation
• Partial or complete disorganization of a protein’s

characteristic three-dimensional shape
– Occurs due to disruption of its secondary, tertiary, and
quaternary structural interactions
• Coagulation - Precipitation out of biochemical
solution of denatured protein
– Example: Egg white is a concentrated solution of
protein albumin, which forms a jelly when heated
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Section 20.15
• Cooking denatures proteins

– Makes it easy for enzymes in our body to
hydrolyze/digest protein
– Kills microorganisms by denaturation of proteins
• A fever of above 106°F is dangerous
– Denatures and inactivates the body’s enzymes, which
function as catalysts
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Section 20.15
What is the consequence of protein denaturation?
a.Partial or complete loss of a protein’s three-dimensional

structure
b.Loss of biochemical activity of the protein
c.Disruption of the secondary, tertiary, and quaternary
structural interactions
d.All the above
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Section 20.15
What is the consequence of protein denaturation?
a.Partial or complete loss of a protein’s three-dimensional

structure
b.Loss of biochemical activity of the protein
c.Disruption of the secondary, tertiary, and quaternary
structural interactions
d.All the above
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Section 20.16
Protein Classification Based on Shape
• Fibrous proteins: Protein molecules with

elongated shape
– One dimension is much longer than the others
– Generally insoluble in water
– Have a single type of secondary structure
– Tend to have simple, regular, and linear structures
– Aggregate together to form macromolecular
structures
• Example: Hair, nails, etc
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Section 20.16
• Globular proteins: Protein molecules with

peptide chains folded into spherical or globular
shapes
– Water soluble substances - Hydrophobic amino acid
residues are in the protein core
• Membrane proteins: Proteins associated with
cell membranes
– Insoluble in water - Hydrophobic amino acid residues
are on the surface
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Section 20.16
Fibrous Proteins: -Keratin

• Provide protective coating for organisms
• Major protein constituent of hair, feather, nails,
horns, and turtle shells
• Mainly made of hydrophobic amino acid
residues
• Individual molecules are almost wholly  helical
– Pairs of these helices twine about one another to
produce a coiled coil
– Coiling at higher levels produces the strength
associated with -keratin-containing proteins
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Section 20.16
Fibrous Proteins: Collagen

• Most abundant protein in humans (30% of total
body protein)
• Major structural material in tendons, ligaments,
blood vessels, and skin
• Organic component of bones and teeth
• Predominant structure - Triple-helix
– Glycine and proline help maintain the structure of the
triple-helix
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Section 20.16
Globular Proteins: Hemoglobin

• An oxygen-carrier molecule in blood
– Transports oxygen from lungs to tissues
• Tetramer (four polypeptide chains)
– Each subunit contains a heme group
• One molecule can transport up to four oxygen
molecules at time
• Iron atom in heme interacts with oxygen
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Section 20.16
Globular Proteins: Myoglobin

• Oxygen-storage molecule in muscles
• Monomer
– Consists of a single peptide chain and one heme unit
– One molecule carries one O2 molecule
• Has a higher affinity for oxygen than hemoglobin
• Oxygen stored in myoglobin molecules serves
as a reserve source for working muscles when
oxygen demand exceeds its supply
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Section 20.16
Aqueous soluble proteins fold into a spherical or

globular shape. Which of the following contains
only soluble proteins?
a.Fibrin, insulin, hemoglobin

b.Myoglobin, myosin, keratin
c.Hemoglobin, insulin, immunoglobulin
d.Elastin, myosin, keratin
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Section 20.16
Aqueous soluble proteins fold into a spherical or

globular shape. Which of the following contains
only soluble proteins?
a.Fibrin, insulin, hemoglobin

b.Myoglobin, myosin, keratin
c.Hemoglobin, insulin, immunoglobulin
d.Elastin, myosin, keratin
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Section 20.17
Protein Classification Based on Function
• Proteins play crucial roles in biochemical

processes
• Diversity of functions exhibited by proteins
exceeds the role of other biochemical molecules
• Functional versatility of proteins stems from their
ability to:
– Bind small molecules specifically and strongly
– Bind other proteins and form fiber-like structures
– Integrate into cell membranes
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Section 20.17
• Catalytic proteins are known for their role as

catalysts
– Almost every chemical reaction in the body is driven
by an enzyme
• Defense proteins are central to functioning of the
body’s immune system
– Known as immunoglobulins or antibodies
• Transport proteins bind to small biomolecules,
transport them to other locations in the body,
and release them as needed
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Section 20.17
• Messenger proteins transmit signals to

coordinate biochemical processes between
different cells, tissues, and organs
– Examples: Insulin, glucagon, and human growth
hormone
• Contractile proteins are necessary for all forms
of movement
– Examples: Actin and myosin
– Human reproduction depends on the movement of
sperm, which is possible because of contractile
proteins
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Section 20.17
• Structural proteins confer stiffness and rigidity

– Collagen is a component of cartilage
– -keratin gives mechanical strength and protective
covering to hair, nails, feathers, and hooves
• Transmembrane proteins control the movement
of small molecules and ions through the cell
membrane
– Have channels to help molecules enter and exit the
cell
– Selective, allow passage of only one type of molecule
or ion
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Section 20.17
• Storage proteins bind (and store) small

molecules
– Ferritin - Iron-storage protein which saves iron for use
in the biosynthesis of new hemoglobin molecules
– Myoglobin - Oxygen-storage protein present in
muscle
• Regulatory proteins are found embedded in the
exterior surface of cell membranes
– Act as sites for receptor molecules
– Bind to enzymes (catalytic proteins) and control
enzymatic action
Return to TOC

Section 20.17
• Nutrient proteins are important in the early

stages of life, from embryo to infant
– Examples: Casein (found in milk) and ovalbumin
(found in egg white)
• Milk provides immunological protection for mammalian
young
• Buffer proteins are part of the system by which
the acid–base balance within body fluids is
maintained
• Fluid-balance proteins maintain fluid balance
between blood and surrounding tissue Return to TOC

Section 20.17
Which of the following proteins plays the role of

biochemical catalysts in the human body?
a.Hormones
b.Enzymes
c.Transferrin
d.Antibodies
Return to TOC

Section 20.17
Which of the following proteins plays the role of

biochemical catalysts in the human body?
a.Hormones
b.Enzymes
c.Transferrin
d.Antibodies
Return to TOC

Section 20.18
Glycoproteins
• Contain carbohydrates or carbohydrate

derivatives in addition to amino acids
– Examples: Proteins in cell membrane and blood
group markers of the ABO system
• Collagen
– Structural feature - 4-hydroxyproline (5%) and 5-
hydroxylysine (1%)
– Carbohydrate units are attached by glycosidic
linkages to collagen at its 5-hydroxylysine residues
• Direct the assembly of collagen triple helices into
collagen fibrils
Return to TOC

Section 20.18
Glycoproteins
Immunoglobulins
• Produced as a protective response to the
invasion of microorganisms or foreign molecules
• Serve as antibodies to combat invasion of the
body by antigens
– Antigen: Foreign substance, such as a bacterium or
virus, that invades the human body
– Antibody: Biochemical molecule that counteracts a
specific antigen
Return to TOC

Section 20.18
Glycoproteins
Immunoglobulins
• Bonding of an antigen to variable regions of
immunoglobulins occurs through hydrophobic
interactions, dipole–dipole interactions, and
hydrogen bonds
Return to TOC

Section 20.18
Glycoproteins
An _____ is a glycoprotein produced by an

organism in response to an invasion of a foreign
substance known as a _____.
a.antibody; antigen
b.antigen, immunoglobulin
c.antigen; antibody
d.antibody; immunoglobulin
Return to TOC

Section 20.18
Glycoproteins
An _____ is a glycoprotein produced by an

organism in response to an invasion of a foreign
substance known as a _____.
a.antibody; antigen
b.antigen, immunoglobulin
c.antigen; antibody
d.antibody; immunoglobulin
Return to TOC

Section 20.19
Lipoproteins
• Conjugated proteins that contain lipids and

amino acids
• Help suspend lipids and transport them through
the bloodstream
• Classes of plasma lipoproteins
– Chylomicrons - Transport dietary triacylglycerols from
intestine to the liver and to adipose tissue
Return to TOC

Section 20.19
Lipoproteins
– Very-low-density lipoproteins (VLDL) - Transport

triacylglycerols synthesized in the liver to adipose
tissue
– Low-density lipoproteins (LDL) - Transport cholesterol
synthesized in the liver to cells throughout the body
– High-density lipoproteins (HDL) - Collect excess
cholesterol from body tissues and transport it back to
the liver for degradation to bile acids
Return to TOC

Section 20.19
Lipoproteins
Which class of plasma lipoproteins is responsible

for transporting cholesterol synthesized in the liver
to cells throughout the body?
a.Chylomicrons
b.Very-low-density lipoproteins (VLDLs)
c.Low-density lipoproteins (LDLs)
d.High-density lipoproteins (HDLs)
Return to TOC

Section 20.19
Lipoproteins
Which class of plasma lipoproteins is responsible

for transporting cholesterol synthesized in the liver
to cells throughout the body?
a.Chylomicrons
b.Very-low-density lipoproteins (VLDLs)
c.Low-density lipoproteins (LDLs)
d.High-density lipoproteins (HDLs)
Return to TOC

Chapter 20
Concept Question 1
The peptide met-gly-phe-ser-ala is known as a _____.
The N-terminal amino acid is _____, and the C-
terminal amino acid is _____. The IUPAC name of this
peptide is _____.
a.pentapeptide; alanine; methionine;
methionineglycinephenylalanineserinealanine
b.hexapeptide; methionine; alanine;
c.hexapeptide; alanine; methionine;
methionylglycylphenylalanylserylalanine
d.pentapeptide; methionine; alanine;
Return to TOC

Chapter 20
Concept Question 1
The peptide met-gly-phe-ser-ala is known as a _____.
The N-terminal amino acid is _____, and the C-
terminal amino acid is _____. The IUPAC name of this
peptide is _____.
a.pentapeptide; alanine; methionine;
b.hexapeptide; methionine; alanine;
c.hexapeptide; alanine; methionine;
d.pentapeptide; methionine; alanine;
Return to TOC

Chapter 20
Concept Question 2
Egg whites are made up of albumin, a single-chain
protein. Why does the albumin solidify when placed in
a hot skillet?
a.Heat causes denaturation of albumin destroying its primary,

secondary, tertiary, and quaternary structures.
b.Heat causes denaturation of albumin destroying its secondary,
tertiary, and quaternary structures.
c.Heat causes denaturation of albumin destroying its secondary
and tertiary structures.
d.Heat causes albumin chains to fuse together through the
formation of new covalent bonds between the chains.
Return to TOC

Chapter 20
Concept Question 2
Egg whites are made up of albumin, a single-chain
protein. Why does the albumin solidify when placed in
a hot skillet?
a.Heat causes denaturation of albumin destroying its primary,

secondary, tertiary, and quaternary structures.
b.Heat causes denaturation of albumin destroying its secondary,
tertiary, and quaternary structures.
c.Heat causes denaturation of albumin destroying its secondary
and tertiary structures.
d.Heat causes albumin chains to fuse together through the
formation of new covalent bonds between the chains.
Return to TOC

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Section 20.

Copyright ©2016 Cengage Learning. All Rights Reserved. 1

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20.11Secondary structure of proteins

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• Protein: Naturally-occurring, unbranched

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Proteins are naturally occurring polymers in which

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Proteins are naturally occurring polymers in which

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Amino Acids: The Building Blocks for Proteins

• Contain both an amino (—NH2) and a carboxyl

Copyright ©2016 Cengage Learning. All Rights Reserved. 7

Amino Acids: The Building Blocks for Proteins

Standard Amino Acids

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Amino Acids: The Building Blocks for Proteins

Polar Amino Acids

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Amino Acids: The Building Blocks for Proteins

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Amino Acids: The Building Blocks for Proteins

Table 20.1 - 20 Standard Amino Acids

Copyright ©2016 Cengage Learning. All Rights Reserved. 11

Amino Acids: The Building Blocks for Proteins

Table 20.1 - 20 Standard Amino Acids

Copyright ©2016 Cengage Learning. All Rights Reserved. 12

Amino Acids: The Building Blocks for Proteins

Table 20.1 - 20 Standard Amino Acids

Copyright ©2016 Cengage Learning. All Rights Reserved. 13

Amino Acids: The Building Blocks for Proteins

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Amino Acids: The Building Blocks for Proteins

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Amino Acids: The Building Blocks for Proteins

Amino acids are organic compounds that contain a

a.hydroxy; carboxyl; -hydroxy amino acids

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Amino Acids: The Building Blocks for Proteins

Amino acids are organic compounds that contain a

a.hydroxy; carboxyl; -hydroxy amino acids

Copyright ©2016 Cengage Learning. All Rights Reserved. 17

Essential Amino Acids

• Standard amino acids needed for protein

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Essential Amino Acids

Incomplete dietary proteins contain inadequate

a.one or more essential amino acids.

Copyright ©2016 Cengage Learning. All Rights Reserved. 19

Essential Amino Acids

Incomplete dietary proteins contain inadequate

a.one or more essential amino acids.

Copyright ©2016 Cengage Learning. All Rights Reserved. 20

Chirality and Amino Acids

• Four different groups are attached to the -

Copyright ©2016 Cengage Learning. All Rights Reserved. 21

Chirality and Amino Acids