PROTEINS

MC 2: Biochemistry
Faisal H. Jackarain, RN, MPH, CLSSYB
Faculty, Manila Doctors College of Nursing
CHARACTERISTICS OF PROTEINS
• 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
CHARACTERISTICS OF PROTEINS
Proteins are naturally occurring polymers in which
the monomer units are _____.
a.triacylglycerols
b.amino acids
c.carbohydrates
d.nucleosides
CHARACTERISTICS OF PROTEINS
Proteins are naturally occurring polymers in which
the monomer units are _____.
a.triacylglycerols
b.amino acids
c.carbohydrates
d.nucleosides
CHARACTERISTICS OF PROTEINS
Amino Acids
• Contain both an amino (—NH2) and a carboxyl (—COOH)
group

–a -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
CHARACTERISTICS OF PROTEINS
Amino Acids
• Contain both an amino (—NH2) and a carboxyl (—COOH) group

–a -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
AMINO ACIDS:
THE BUILDING BLOCKS FOR PROTEINS
Standard Amino Acids
• 20 a-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
 AMINO ACIDS:
THE BUILDING BLOCKS FOR PROTEINS
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
AMINO ACIDS:
THE BUILDING BLOCKS FOR PROTEINS
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
 AMINO ACIDS:
THE BUILDING BLOCKS FOR PROTEINS
Table 20.1 - 20 Standard Amino Acids
 AMINO ACIDS:
THE BUILDING BLOCKS FOR PROTEINS
Table 20.1 - 20 Standard Amino Acids
 AMINO ACIDS:
THE BUILDING BLOCKS FOR PROTEINS
Table 20.1 - 20 Standard Amino Acids
AMINO ACIDS:
THE BUILDING BLOCKS FOR PROTEINS
Practice Exercise
• Classify the following amino acids based on the
polarity of their R-groups.
AMINO ACIDS:
THE BUILDING BLOCKS FOR PROTEINS
Practice Exercise
• Classify the following amino acids based on the
polarity of their R-groups.
AMINO ACIDS:
THE BUILDING BLOCKS FOR PROTEINS
Amino acids are organic compounds that contain a
_____ group and a _____ group and are found in
proteins as _____.
a.hydroxy; carboxyl; a-hydroxy amino acids
b.amino; carboxyl; a-amino acids
c.amino; carboxyl; beta amino acids
d.hydroxy; carboxyl; beta hydroxy amino acids
AMINO ACIDS:
THE BUILDING BLOCKS FOR PROTEINS
Amino acids are organic compounds that contain a
_____ group and a _____ group and are found in
proteins as _____.
a.hydroxy; carboxyl; a-hydroxy amino acids
b.amino; carboxyl; a-amino acids
c.amino; carboxyl; beta amino acids
d.hydroxy; carboxyl; beta hydroxy amino acids
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
ESSENTIAL AMINO ACIDS
• Complete Dietary Protein: Contains all essential
amino acids
• Incomplete Dietary Protein: Does not contain
adequate amounts, relative to the body’s needs of
one or more essential amino acids
• Complementary Dietary Protein: combination of
two or more incomplete dietary protein that provides
an adequate amount of essential amino acids
ESSENTIAL AMINO ACIDS
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.
ESSENTIAL AMINO ACIDS
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.
CHIRALITY AND AMINO ACIDS
• Four different groups are attached to the a- 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)
CHIRALITY AND AMINO ACIDS
• 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
CHIRALITY AND AMINO ACIDS
– 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
 CHIRALITY AND AMINO ACIDS

– 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
Name the following amino acids with correct
designation for the enantiomer (chiral carbon is
indicated by *)
Name the following amino acids with correct
designation for the enantiomer (chiral carbon is
indicated by *)

A = L-isoleucine B = D-cysteine C = L-tyrosine

With few exceptions, the amino acids found in
nature and in proteins are _____ isomers.
a.alpha
b.beta
c.ᴅ
d.ʟ
With few exceptions, the amino acids found in
nature and in proteins are _____ isomers.
a.alpha
b.beta
c.ᴅ
d.ʟ
ACID–BASE PROPERTIES OF AMINO ACIDS
• In pure form, amino acids are white crystalline solids
– Decompose before they melt
• Not very soluble in water
• a-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
ACID–BASE PROPERTIES OF AMINO ACIDS
• 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
ACID–BASE PROPERTIES OF AMINO ACIDS
ACID–BASE PROPERTIES OF AMINO ACIDS
• pH at which an amino acid exists in its zwitterion
form
– Carries zero net charge
• Different amino acids have different isoelectric points
ACID–BASE PROPERTIES OF AMINO ACIDS
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
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
CYSTEINE:
A CHEMICALLY UNIQUE AMINO ACID
 CYSTEINE:
A CHEMICALLY UNIQUE AMINO ACID

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
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
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 Nterminal
amino acid residue
• Example: Ala-leu-gly has the IUPAC name of
alanylleucylglycine
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
PEPTIDES

How many isomeric peptides are possible from a

peptide of four different amino acids?

a.8
b.12
c.16
d.24
PEPTIDES

How many isomeric peptides are possible from a

peptide of four different amino acids?

a.8
b.12
c.16
d.24
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
BIOCHEMICALLY IMPORTANT SMALL PEPTIDES
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
BIOCHEMICALLY IMPORTANT SMALL PEPTIDES
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
BIOCHEMICALLY IMPORTANT SMALL PEPTIDES
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
BIOCHEMICALLY IMPORTANT SMALL PEPTIDES

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
BIOCHEMICALLY IMPORTANT SMALL PEPTIDES

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
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
GENERAL STRUCTURAL
CHARACTERISTICS OF PROTEINS
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
 GENERAL STRUCTURAL
CHARACTERISTICS OF PROTEINS

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
 GENERAL STRUCTURAL
CHARACTERISTICS OF PROTEINS

– 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
 GENERAL STRUCTURAL
CHARACTERISTICS OF PROTEINS

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
 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
PRIMARY STRUCTURE OF
PROTEINS

Figure 20.4 - Primary

Structure of a Human
Myoglobin
PRIMARY STRUCTURE OF PROTEINS
• 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
PRIMARY STRUCTURE OF PROTEINS
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
 PRIMARY STRUCTURE OF PROTEINS

The order in which amino acids are linked in a

protein is known as the _____ structure.
a.primary
b.secondary
c.tertiary
d.quaternary
 PRIMARY STRUCTURE OF PROTEINS

The order in which amino acids are linked in a

protein is known as the _____ structure.
a.primary
b.secondary
c.tertiary
d.quaternary
SECONDARY STRUCTURE OF PROTEINS
• Arrangement in space adopted by the backbone
portion of a protein
• Types - Alpha-helix (a helix) and the betapleated
sheet (b 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
SECONDARY STRUCTURE OF PROTEINS
– 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.
SECONDARY STRUCTURE OF PROTEINS
• 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
 SECONDARY STRUCTURE OF PROTEINS

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
 SECONDARY STRUCTURE OF PROTEINS

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
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
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
Figure 20.13 - Stabilizing Influences that Contribute to the Tertiary Structure
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
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
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
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
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
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
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.
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.
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
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
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
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
• 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
• 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
FIBROUS PROTEINS: AKERATIN

• 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 a helical
– Pairs of these helices twine about one another to produce
a coiled coil
– Coiling at higher levels produces the strength associated
with a-keratin-containing proteins
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
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
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
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
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
• 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
• 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
• 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
• Structural proteins confer stiffness and rigidity
– Collagen is a component of cartilage
– a-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
• 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
• 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
Which of the following proteins plays the role of biochemical
catalysts in the human body?
a.Hormones
b.Enzymes
c.Transferrin
d.Antibodies
• 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
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
Immunoglobulins
• Bonding of an antigen to variable regions of immunoglobulins
occurs through hydrophobic interactions, dipole–dipole
interactions, and hydrogen bonds
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
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
• 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
– 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
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)
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)
Concept Question 1
The peptide met-gly-phe-ser-ala is known as a _____. The N-terminal
amino acid is _____, and the Cterminal amino acid is _____. The
IUPAC name of this peptide is _____.
a.pentapeptide; alanine; methionine;
methionineglycinephenylalanineserinealanine
b.hexapeptide; methionine; alanine;
methionineglycinephenylalanineserinealanine
c.hexapeptide; alanine; methionine;
methionylglycylphenylalanylserylalanine
d.pentapeptide; methionine; alanine;
methionylglycylphenylalanylserylalanine
Concept Question 1
The peptide met-gly-phe-ser-ala is known as a _____. The N-terminal
amino acid is _____, and the Cterminal amino acid is _____. The
IUPAC name of this peptide is _____.
a.pentapeptide; alanine; methionine;
methionineglycinephenylalanineserinealanine
b.hexapeptide; methionine; alanine;
methionineglycinephenylalanineserinealanine
c.hexapeptide; alanine; methionine;
methionylglycylphenylalanylserylalanine
d.pentapeptide; methionine; alanine;
methionylglycylphenylalanylserylalanine
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.
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.