CHAPTER III

PROTEINS

Prepared by:
Prof. Nemia T. Dacumos

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An amino acid is an organic compound that contains both an amino (-NH2) group and a
carboxyl (-COOH) group. The amino acids found in proteins are always α-amino acids. An
-amino acid is an amino acid in which the amino group and the carboxyl group are
attached to the α -carbon atom. The general structural formula for an α -amino acid is

The R group present in an α -amino acid is called the amino acid side chain. The nature
of this side chain distinguishes α -amino acids from each other. Side chains vary in size,
shape, charge, acidity, functional groups present, hydrogen-bonding ability, and
chemical reactivity.
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Over 700 different naturally occurring amino acids are known, but only 20 of them,
called standard amino acids, are normally present in proteins. A standard amino acid
is one of the 20 α-amino acids normally found in proteins. The structures of the 20
standard amino acids are given in Table 20.1.

Within Table 20.1, amino acids are grouped according to side-chain polarity. In this
system there are four categories: (1) nonpolar amino acids, (2) polar neutral amino
acids, (3) polar acidic amino acids, and (4) polar basic amino acids. This classification
system gives insights into how various types of amino acid side chains help determine
the properties of proteins.

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A nonpolar amino acid is an amino acid that contains one amino group, one carboxyl
group, and a nonpolar side chain. When incorporated into a protein, such amino acids
are hydrophobic (“water-fearing”); that is, they are not attracted to water molecules.
They are generally found in the interior of proteins, where there is limited contact with
water. There are nine nonpolar amino acids. Tryptophan is a borderline member of this
group because water can weakly interact through hydrogen bonding with the NH ring
location on tryptophan’s side-chain ring structure. Thus, some textbooks list
tryptophan as a polar neutral amino acid.

The nonpolar amino acid proline has a

structural feature not found in any other
standard amino acid. Its side chain, a propyl
group, is bonded to both the α-carbon atom
and the amino nitrogen atom, giving a cyclic
side chain.
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 Chirality and Amino Acids

Four different groups are attached to the a-carbon atom in all of the standard amino
acids except glycine, where the R group is a hydrogen atom.

Glycine, the simplest of the standard amino acids, is achiral. All of the other
standard amino acids are chiral.

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This means that the structures of 19 of the 20 standard amino acids possess a chiral
center at this location, so enantiomeric forms exist for each of these amino acids.
With few exceptions (in some bacteria), the amino acids found in nature and in
proteins are L isomers. Thus, as is the case with monosaccharides, nature favors one
mirror-image form over the other. Interestingly, for amino acids the L isomer is the
preferred form, whereas for monosaccharides the D isomer is preferred.

The rules for drawing Fischer projection formulas for amino acid structures follow.

1. The —COOH group is put at the top of the projection, the R group at the bottom.
This positions the carbon chain vertically.

2. The —NH2 group is in a horizontal position. Positioning it on the left denotes the L
isomer, and positioning it on the right denotes the D isomer.
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Acid-Base Properties of Amino Acids

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Such a molecule is known as a zwitterion, from the German term meaning “double ion.” A zwitterion
is a molecule that has a positive charge on one atom and a negative charge on another atom, but 16
which has no net charge.
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The ability of amino acids to react with both H3O+ and OH- ions means that amino
acid solutions can function as buffers. The same is true for proteins, which are
amino acid polymers. The buffering action of proteins present in blood is a major
function of such proteins.

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The previous discussion assumed that the side chain (R group) of an amino acid
remains unchanged in solution as the pH is varied. This is the case for neutral amino
acids but not for acidic or basic ones. For these latter compounds, the side chain can
also acquire a charge because it contains an amino or a carboxyl group that can,
respectively, gain or lose a proton.

Because of the extra site that can be protonated or deprotonated, acidic and basic
amino acids have four charged forms in solution. These four forms for aspartic acid,
one of the acidic amino acids, are

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• The existence of two low-pH forms for aspartic acid results from the two carboxyl
groups being deprotonated at different pH values.
• For basic amino acids, two high-pH forms exist because deprotonation of the
amino groups does not occur simultaneously.
• The side-chain amino group deprotonates before the α-amino group for histidine,
but the opposite is true for lysine and arginine.

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• The amounts of the various forms of an amino acid — zwitterion, negative ion(s), and
positive ion(s) — that are present in an aqueous solution of the amino acid vary with
solution pH.
• There is no pH at which ionic amino acid forms are absent, but there is a pH at which
there is an equal number of positive and negative charges present, which produces a
“no net charge” situation.
• The “no net charge” pH value for an amino acid solution is called its isoelectric point.
• An isoelectric point is the pH at which an amino acid solution has no net charge
because an equal number of positive and negative charges are present.
• At the isoelectric point, almost all amino acid molecules in a solution (more than 99%)
are present in their zwitterion form.

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Practice Exercise

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Practice Exercise

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Cysteine

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 Peptides
Under proper conditions, amino acids can bond together to produce an unbranched
chain of amino acids. The length of the amino acid chain can vary from a few amino acids
to many amino acids. Representative of such chains is the following five-amino-acid
chain.

Such a chain of covalently linked amino acids is called a peptide. A peptide is an

unbranched chain of amino acids, each joined to the next by a peptide bond. Peptides are
further classified by the number of amino acids present in the chain. A compound
containing two amino acids is specifically called a dipeptide; three amino acids joined
together in a chain constitute a tripeptide; and so on. The name oligopeptide is loosely
used to refer to peptides with 10 to 20 amino acid residues, and the name polypeptide is
used to refer to longer peptides. A polypeptide is a long unbranched chain of amino acids,
each joined to the next by a peptide bond
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Nature of the Peptide Bond

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• In amino acid chemistry, amide bonds that link amino acids together are given the
specific name of peptide bond.
• A peptide bond is a covalent bond between the carboxyl group of one amino acid and
the amino group of another amino acid.
• In all peptides, long or short, the amino acid at one end of the amino acid sequence
has a free H3N+ group, and the amino acid at the other end of the sequence has a free
COO- group.
• The end with the free H3N+ group is called the N-terminal end, and the end with the
free COO- group is called the C-terminal end.
• By convention, the sequence of amino acids in a peptide is written with the N-terminal
end amino acid on the left.
• The individual amino acids within a peptide chain are called amino acid residues.
• An amino acid residue is the portion of an amino acid structure that remains, after the
release of H2O, when an amino acid participates in peptide bond formation as it
becomes part of a peptide chain. 37
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 Peptide Nomenclature

IUPAC rules for naming small peptides are as follows:

Rule 1: The C-terminal amino acid residue (located at the far right of the structure)
keeps its full amino acid name.

Rule 2: All of the other amino acid residues have names that end in -yl. The -yl suffix
replaces the -ine or -ic acid ending of the amino acid name, except for tryptophan
(tryptophyl), cysteine (cysteinyl), glutamine (glutaminyl), and asparagine (asparaginyl).

Rule 3: The amino acid naming sequence begins at the N-terminal amino acid residue.

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Isomeric Peptides
Peptides that contain the same amino acids but 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 one molecule
of glycine.

These two compounds are isomers with different chemical and physical properties.
The number of isomeric peptides increases rapidly as the length of the peptide
chain increases.

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 Biochemically Important Small Peptides

Small Peptide Hormones

The two best-known peptide hormones, both produced by the pituitary gland, are
oxytocin and vasopressin. Each hormone is a nonapeptide (nine amino acid residues)
with six of the residues held in the form of a loop by a disulfide bond formed from the
interaction of two cysteine residues. Structurally, these nonapeptides differ in the amino
acid present in positions 3 and 8 of the peptide chain. In both structures, an amide
group replaces the C terminal single-bonded oxygen atom.

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• Oxytocin regulates uterine contractions and lactation. Oxytocin plays a role in
stimulating the flow of milk in a nursing mother. The baby’s suckling action sends
nerve signals to the mother’s brain, triggering the release of oxytocin, via the blood, to
the mammary glands. The oxytocin causes muscle contraction in the mammary gland,
forcing out milk. As suckling continues, more oxytocin is released and more milk is
available for the baby.

• Vasopressin regulates the excretion of water by the kidneys; it also affects blood
pressure.

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Small Peptide Neurotransmitters
Enkephalins are pentapeptide neurotransmitters produced by the brain itself that
bind at receptor sites in the brain to reduce pain. The two best-known enkephalins
are Met-enkephalin and Leu-enkephalin, whose structures are

Met-enkephalin: Tyr–Gly–Gly–Phe–Met
Leu-enkephalin: Tyr–Gly–Gly–Phe–Leu

• The two enkephalins differ structurally only in the amino acid at the end of the
chain.
• The pain-reducing effects of enkephalin action play a role in the “high” reported
by long-distance runners, in the competitive athlete’s managing to finish the
game despite being injured, and in the pain-relieving effects of acupuncture.
• The action of the prescription painkillers morphine and codeine is based on their
binding at the same receptor sites in the brain as the naturally occurring
enkephalins. 48
 Small Peptide Antioxidants
• The tripeptide glutathione (Glu–Cys–Gly) is present in significant concentrations in
most cells and is of considerable physiological importance as a regulator of
oxidation–reduction reactions. Specifically, glutathione functions as an antioxidant,
protecting cellular contents from oxidizing agents such as peroxides and superoxides
(highly reactive forms of oxygen often generated within the cell in response to
bacterial invasion) .
• The tripeptide structure of glutathione has an unusual feature. The amino acid Glu,
an acidic amino acid, is bonded to Cys through the side-chain carboxyl group rather
than through its α-carbon carboxyl group

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 General Structural Characteristics of Proteins
• A protein is a peptide in which at least 40 amino acid residues are present and as a
naturally occurring, unbranched polymer with the amino acids as the monomer.

• The terms polypeptide and protein are often used interchangeably; a protein is a
relatively long polypeptide.

• The key point is that the term protein is reserved for peptides with a large number
of amino acids; it is not correct to call a tripeptide a protein. Over 10,000 amino acid
residues are present in several proteins; 400–500 amino acid residues are common
in proteins; small proteins contain 40–100 amino acid residues.

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Proteins based on peptide chains

A monomeric protein is a protein in which only one peptide chain is present. Large
proteins, those with many amino acid residues, usually are multimeric.

A multimeric protein is a protein in which more than one peptide chain is present.
The peptide chains present in multimeric proteins are called protein subunits. The
protein subunits within a multimeric protein may all be identical to each other or
different kinds of subunits may be present.

Proteins with up to 12 subunits are known. The small protein insulin, which functions
as a hormone in the human body, is a multimeric protein with two protein subunits;
one subunit contains 21 amino acid residues and the other 30 amino acid residues.

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 Proteins based on chemical composition

A simple protein is a protein in which only amino acid residues are present. More than one
protein subunit may be present in a simple protein, but all subunits contain only amino
acids.

A conjugated protein is a protein that has one or more non-amino acid entities present in
its structure in addition to one or more peptide chains. These non-amino acid components,
which may be organic or inorganic, are called prosthetic groups. A prosthetic group is a
non-amino acid group present in a conjugated protein.

Conjugated proteins may be further classified according to the nature of the prosthetic
group (s) present. Lipoproteins contain lipid prosthetic groups, glycoproteins contain
carbohydrate groups, metalloproteins contain a specific metal, and so on (see Table 20.3).

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 Protein Structural Level
• Primary protein structure is the order in which amino acids are linked together in a
protein. Every protein has its own unique amino acid sequence. Primary protein
structure always involves more than just the numbers and kinds of amino acids
present; it also involves the order of attachment of the amino acids to each other
through peptide bonds.
• Insulin, the hormone that regulates blood-glucose levels, was the first protein for
which primary structure was determined; the “sequencing” of its 51 amino acids was
completed in 1953, after 8 years of work by the British biochemist Frederick Sanger
(see Figure 20.3). Today, primary structures are known for many thousands of proteins,
and the sequencing procedures involve automated methods that require relatively
short periods of time (days).
• Figure 20.4 shows the primary structure of myoglobin, a protein involved in oxygen
transport in muscles; it contains 153 amino acids assembled in the particular, definite
order shown in this diagram.
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 Insulin

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The primary structure of human myoglobin. This
diagram gives only the sequence of the amino
acids present and conveys no information about
the actual three-dimensional shape of the protein.
The “wavy” pattern for the 153 amino acid
sequence was chosen to minimize the space used
to present the needed information. The actual
shape of the protein is determined by secondary
and tertiary levels of protein structure, levels yet to
be discussed

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An analogy is often drawn between the primary structure of proteins and words. Words,
which convey information, are formed when the 26 letters of the English alphabet are
properly sequenced. Proteins are formed from proper sequences of the 20 standard
amino acids. Just as the proper sequence of letters in a word is necessary for it to make
sense, the proper sequence of amino acids is necessary to make biochemically active
protein. Furthermore, the letters that form a word are written from left to right, as are
amino acids in protein formulas.

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• Secondary protein structure is the arrangement in space adopted by the backbone
portion of a protein.
• The two most common types of secondary structure are the alpha helix ( α-helix) and
the beta pleated sheet (β-pleated sheet).
• The type of interaction responsible for both of these types of secondary structure is
hydrogen bonding (Section 7.13) between a carbonyl oxygen atom of a peptide
linkage and the hydrogen atom of an amino group of another peptide linkage farther
along the backbone.
• Information about the geometry associated with these peptide linkages is helpful in
understanding how hydrogen bonding interactions occur between peptide linkages of
a protein backbone.

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 Important geometrical considerations are

1. The peptide linkages are essentially planar. This means that for two amino acids linked
through a peptide linkage, six atoms lie in the same plane: the α-carbon atom and the C = O
group from the first amino acid and the N–H group and the α -carbon atom from the second
amino acid.

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2. The planar peptide linkage structure has considerable rigidity, which means that
rotation of groups about the C- N bond is hindered, and cis–trans isomerism is possible
about this bond. The trans isomer orientation is the preferred orientation, as shown in
the preceding diagram. The O atom of the C = O group and the H atom of the N -H
group are positioned trans to each other

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The Alpha Helix

• An alpha helix structure is a protein secondary structure in which a single protein chain
adopts a shape that resembles a coiled spring (helix), with the coil configuration
maintained by hydrogen bonds.

• The hydrogen bonds are between N-H and C= O groups of every fourth amino acid, as is
shown diagrammatically in Figure 20.6.

• Proteins have varying amounts of α-helical secondary structure, ranging from a few
percent to nearly 100%. In an a helix, all of the amino acid side chains (R groups) lie
outside the helix; there is not enough room for them in the interior. Figure 20.6d
illustrates this situation.

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Four representations of the α-helix protein secondary structure. (a) Arrangement of protein
backbone with no detail shown. (b) Backbone arrangement with hydrogen-bonding interactions
shown. (c) Backbone atomic detail shown, as well as hydrogen-bonding interactions. (d) Top view
of an α- helix showing that amino acid side chains (R groups) point away from the long axis of the
helix. 64
The Beta Pleated Sheet

• A beta pleated sheet structure is a protein secondary structure in which two fully
extended protein chain segments in the same or different molecules are held
together by hydrogen bonds.

• Hydrogen bonds form between oxygen and hydrogen peptide linkage atoms that
are either in different parts of a single chain that folds back on itself (intrachain
bonds) or between atoms in different peptide chains in those proteins that contain
more than one chain (interchain bonds).

• In molecules where the pleated sheet involves a single molecule, several U-turns in
the protein chain arrangement are needed in order to form the structure.

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This “U-turn structure” is the most frequently encountered type of pleated sheet
structure

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Figure 20.7a shows a representation of the pleated sheet structure that occurs when portions of two
different peptide chains are aligned parallel to each other (interchain bonds). The term pleated sheet
arises from the repeated zigzag pattern in the structure (Figure 20.7b). Note how in a pleated sheet
structure the amino acid side chains are positioned above and below the plane of the sheet.

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The β-pleated sheet is found extensively in the protein of silk. Because such proteins
are already fully extended, silk fibers cannot be stretched. When wool, which has an
helix structure, becomes wet, it stretches as hydrogen bonds of the helix are broken.
The wool returns to its original shape as it dries. Wet stretched wool, dried under
tension, maintains its stretched length because it has assumed a β-pleated sheet
configuration.

Structure of Silk
Protein

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• Tertiary protein structure is the overall three-dimensional shape of a protein that
results from the interactions between amino acid side chains (R groups) that are widely
separated from each other within a peptide chain.
• A good analogy for the relationships among the primary, secondary, and tertiary
structures of a protein is that of a telephone cord (Figure 20.9). The primary structure is
the long, straight cord. The coiling of the cord into a helical arrangement gives the
secondary structure. The supercoiling arrangement the cord adopts after you hang up
the receiver is the tertiary structure.

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Interactions Responsible for Tertiary Structure

• Four types of attractive interactions contribute to the tertiary structure of a protein:

(1) covalent disulfide bonds, (2) electrostatic attractions (salt bridges), (3) hydrogen
bonds, and (4) hydrophobic attractions.
• All four of these interactions are interactions between amino acid R groups. This is a
major distinction between tertiary-structure interactions and secondary-structure
interactions.
• Tertiary-structure interactions involve the R groups of amino acids; secondary-
structure interactions involve the peptide linkages between amino acid residues.

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Disulfide bonds, the strongest of the tertiary-structure interactions, result from the -SH
groups of two cysteine residues reacting with each other to form a covalent disulfide bond
(Section 20.5). This type of interaction is the only one of the four tertiary-structure
interactions that involves a covalent bond. Disulfide bond formation may involve two
cysteine units in the same peptide chain (an intramolecular disulfide bond; see Figure
20.10a) or two cysteine units in different chains (an intermolecular disulfide bond; see
Figure 20.10b). Figure 20.11 gives the structure of the protein hormone insulin, a protein
that has two peptide chains and a total of 51 amino acid residues; both inter- and
intramolecular disulfide bonds are present in its structure. 72
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Electrostatic interactions, also called salt bridges, always involve the interaction
between an acidic side chain (R group) and a basic side chain (R group). The side
chains of acidic and basic amino acids, at the appropriate pH, carry charges, with the
acidic side chain being negatively charged and the basic side chain being positively
charged.

Such side chain charges occur when a —COOH group becomes a –COO- group and
when a —NH2 group becomes a —NH3+group. The interaction that occurs between
the two types of side chains is a positive–negative ion–ion attraction. Figure 20.12b
shows an electrostatic interaction.

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Hydrogen bonds can occur between amino acids with polar R groups. A variety of polar
side chains can be involved, especially those that possess the following functional
groups:

Hydrophobic interactions result when two nonpolar side chains are close to each other.
In aqueous solution, many proteins have their polar R groups outward, toward the
aqueous solvent (which is also polar), and their nonpolar R groups inward (away from
the polar water molecules).

The nonpolar R groups then interact with each other. The attractive forces are London
forces (Section 7.13) resulting from the momentary uneven distribution of electrons
within the side chains.
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In 1959, a protein tertiary structure
was determined for the first time.
The determination involved
myoglobin, a conjugated protein
(Section 20.8) whose function is
oxygen storage in muscle tissue.
Figure 20.13 shows myoglobin’s
tertiary structure. It involves a single
peptide chain of 153 amino acids
with numerous α-helix segments
within the chain. The structure also
contains a prosthetic heme group, an
iron-containing group with the ability
to bind molecular oxygen.
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• Quaternary structure is the highest level of protein organization. It is found only in
multimeric proteins (Section 20.8). Such proteins have structures involving two or
more peptide chains that are independent of each other — that is, are not covalently
bonded to each other.
• Quaternary protein structure is the organization among the various peptide chains in
a multimeric protein.
• Most multimeric proteins contain an even number of subunits (two subunits = dimer,
four subunits = tetramer, and so on). The subunits are held together mainly by
hydrophobic interactions between amino acid R groups.
• The noncovalent interactions that contribute to tertiary structure (electrostatic
interactions, hydrogen bonds, and hydrophobic interactions) are also responsible for
the maintenance of quaternary structure. The noncovalent interactions that
contribute to quaternary structure are, however, more easily disrupted.

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For example, only small changes in cellular conditions can cause a tetrameric protein
to fall apart, dissociating into dimers or perhaps four separate subunits, with a
resulting temporary loss of protein activity. As original cellular conditions are
restored, the tertiary structure automatically re-forms, and normal protein function is
restored.

An example of a protein with quaternary structure is hemoglobin, the oxygen-

carrying protein in blood (Figure 20.14). It is a tetramer in which there are two
identical a chains and two identical β chains. Each chain enfolds a heme group, the
site where oxygen binds to the protein.

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 Protein Classification based on shape
A fibrous protein is a protein whose molecules have an elongated shape with one dimension
much longer than the others. Fibrous proteins tend to have simple, regular, linear structures.

A globular protein is a protein whose molecules have peptide chains that are folded into
spherical or globular shapes. The folding in such proteins is such that most of the amino acids
with hydrophobic side chains (nonpolar R groups) are in the interior of the molecule and
most of the hydrophilic side chains (polar R groups) are on the outside of the molecule.
Generally, globular proteins are water-soluble substances.

A membrane protein is a protein that is found associated with a membrane system of a cell.
Membrane protein structure is somewhat opposite that of globular proteins, with most of
the hydrophobic amino acid side chains oriented outward. Thus, such proteins tend to be
water-insoluble and they usually have fewer hydrophobic amino acids than globular proteins.
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α-Keratin

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Collagen

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Myoglobin

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Protein Classification based on Function

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 Protein Hydrolysis
When a protein or smaller peptide in a solution of strong acid or strong base is heated, the
peptide bonds of the amino acid chain are hydrolyzed and free amino acids are produced.
The hydrolysis reaction is the reverse of the formation reaction for a peptide bond. Amine
and carboxylic acid functional groups are regenerated

Let us consider the hydrolysis of the tripeptide Ala–Gly–Cys under acidic conditions.
Complete hydrolysis produces one unit each of the amino acids alanine, glycine, and
cysteine. The equation for the hydrolysis is

Note that the product amino acids in this reaction are written in positive-ion form because of the acidic94
reaction conditions.
Protein Denaturation

Protein denaturation is the partial or complete disorganization of a protein’s

characteristic three-dimensional shape as a result of disruption of its secondary, tertiary,
and quaternary structural interactions. Because the biochemical function of a protein
depends on its three-dimensional shape, the result of denaturation is loss of biochemical
activity.

Protein denaturation does not affect the primary structure of a protein. Although some
proteins lose all of their three-dimensional structural characteristics upon denaturation
(Figure 20.19), most proteins maintain some three-dimensional structure. Often, for
limited denaturation changes, it is possible to find conditions under which the effects of
denaturation can be reversed; this restoration process, in which the protein is “refolded,”
is called renaturation. However, for extensive denaturation changes, the process is
usually irreversible. 95
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Loss of water solubility is a frequent physical
consequence of protein denaturation. The
precipitation out of biochemical solution of
denatured protein is called coagulation.

A most dramatic example of protein

denaturation occurs when egg white (a
concentrated solution of the protein albumin) is
poured onto a hot surface. The clear albumin
solution immediately changes into a white solid
with a jelly-like consistency (see Figure 20.20). A
similar process occurs when hamburger juices
encounter a hot surface. A brown jelly-like solid
forms.
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Collagen

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The presence of carbohydrate units (mostly glucose, galactose, and their disaccharides)
attached by glycosidic linkages (Section 18.13) to collagen at its 5-hydroxylysine residues
causes collagen to be classified as a glycoprotein. The function of the carbohydrate groups
in collagen is related to cross-linking; they direct the assembly of collagen triple helices
into more complex aggregations called collagen fibrils.

When collagen is boiled in water, under basic conditions, it is converted to the water-
soluble protein gelatin. This process involves both denaturation (Section 20.15) and
hydrolysis (Section 20.14). Heat acts as a denaturant, causing rupture of the hydrogen
bonds supporting collagen’s triple-helix structure. Regions in the amino acid chains where
proline and hydroxyproline concentrations are high are particularly susceptible to
hydrolysis, which breaks up the polypeptide chains. Meats become more tender when
cooked because of the conversion of some collagen to gelatin. Tougher cuts of meat (more
cross-linking), such as stew meat, need longer cooking times.
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Immunoglobulins

An immunoglobulin is a glycoprotein produced by an organism as a protective response

to the invasion of microorganisms or foreign molecules. Different classes of
immunoglobulins, identified by differing carbohydrate content and molecular mass,
exist.

Immunoglobulins serve as antibodies to combat invasion of the body by antigens. An

antigen is a foreign substance, such as a bacterium or virus, that invades the human
body. An antibody is a biochemical molecule that counteracts a specific antigen. The
immune system of the human body has the capability to produce immunoglobulins that
respond to several million different antigens.

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All types of immunoglobulin molecules have much the same basic structure, which
includes the following features:

1. Four polypeptide chains are present: two identical heavy (H) chains and two
identical light (L) chains.
2. The H chains, which usually contain 400–500 amino acid residues, are
approximately twice as long as the L chains.
3. Both the H and L chains have constant and variable regions. The constant regions
have the same amino acid sequence from immunoglobulin to immunoglobulin, and
the variable regions have a different amino acid sequence in each immunoglobulin.
4. The carbohydrate content of various immunoglobulins varies from 1% to 12% by
mass.
5. The secondary and tertiary structures are similar for all immunoglobulins. They
involve a Y-shaped conformation (Figure 20.22) with disulfide linkages between H
and L chains stabilizing the structure 106
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The interaction of an immunoglobulin molecule with an antigen occurs at the “tips”
(uppermost part) of the Y structure. These tips are the variable-composition region of
the immunoglobulin structure. It is here that the antigen binds specifically, and it is
here that the amino acid sequence differs from one immunoglobulin to another.

Each immunoglobulin has two identical active sites and can thus bind to two
molecules of the antigen it is “designed for.” The action of many such
immunoglobulins of a given type in concert with each other creates an antigen–
antibody complex that precipitates from solution (Figure 20.23). Eventually, an
invading antigen can be eliminated from the body through such precipitation. The
bonding of an antigen to the variable region of an immunoglobulin occurs through
hydrophobic interactions, dipole–dipole interactions, and hydrogen bonds rather than
covalent bonds

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Lipoproteins
A lipoprotein is a conjugated protein that contains lipids in addition to amino acids.
The major function of such proteins is to help suspend lipids and transport them
through the bloodstream. Lipids, in general, are insoluble in blood (an aqueous
medium) because of their nonpolar nature.

A plasma lipoprotein is a lipoprotein that is involved in the transport system for lipids
in the bloodstream. These proteins have a spherical structure that involves a central
core of lipid material (triacylglycerols and cholesterol esters) surrounded by a shell
(membrane structure) of phospholipids, cholesterol, and proteins.

In the blood, cholesterol exists primarily in the form of cholesterol esters formed
from the esterification of cholesterol’s hydroxyl group with a fatty acid.

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There are four major classes of plasma lipoproteins:

1. Chylomicrons. Their function is to transport dietary triacylglycerols from the

intestine to the liver and to adipose tissue.

2. Very low-density lipoproteins (VLDL). Their function is to transport

triacylglycerols synthesized in the liver to adipose tissue.

3. Low-density lipoproteins (LDL). Their function is to transport cholesterol

synthesized in the liver to cells throughout the body.

4. High-density lipoproteins (HDL). Their function is to collect excess cholesterol

from body tissues and transport it back to the liver for degradation to bile acids.

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REFERENCE

General, Organic and Biological Chemistry, H. Stephen Stoker. 5th edition.

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