Protein (Part 1)

CHS 214
Lecture 4
 Lecture’s outline:

n The Chemist’s View of Proteins

n Digestion and Absorption of Protein
n Proteins in the Body
n Protein in Foods
n Health Effects and Recommended Intakes of Protein

CHS 214 – Madawi Aldhwayan 2

 The Chemist’s View of Proteins

proteins contain the same atoms as carbohydrates and lipids—

carbon (C), hydrogen (H), and oxygen (O)—but proteins also
contain nitrogen (N) atoms.

n These nitrogen atoms give the name amino (nitrogen

containing) to the amino acids—the links in the chains of
proteins.

CHS 214 – Madawi Aldhwayan 3

 The Chemist’s View of Proteins

Amino acids:
n All amino acids have the same basic structure—a central
carbon (C) atom with a hydrogen atom (H), an amino group
(NH2), and an acid group (COOH) attached to it.

n Carbon atoms need to form four bonds, this fourth site

distinguishes each amino acid from the others. Attached to the
carbon atom at the fourth bond is a distinct atom, or group of
atoms, known as the side group or side chain

CHS 214 – Madawi Aldhwayan 4

 The Chemist’s View of Proteins

Unique Side Groups:

n The side groups on amino acids vary from one amino acid to
the next, making proteins more complex than either
carbohydrates or lipids.

n A protein is made up of about 20 different amino acids, each

with a different side group.

CHS 214 – Madawi Aldhwayan 5

 The Chemist’s View of Proteins

A. Nonessential Amino Acids

n More than half of the amino acids are nonessential, meaning
that the body can synthesize them for itself.

n Proteins in foods usually deliver these amino acids, but it is not

essential that they do so. The body can make all nonessential
amino acids, given nitrogen to form the amino group and
fragments from carbohydrate or fat to form the rest of the
structure.

CHS 214 – Madawi Aldhwayan 6

 The Chemist’s View of Proteins

B. Essential Amino Acids

n There are nine amino acids that the human body either cannot
make at all or cannot make in sufficient quantity to meet its
needs.

n They must be supplied by the diet; they are essential.

CHS 214 – Madawi Aldhwayan 7

CHS 214 – Madawi Aldhwayan 8
 The Chemist’s View of Proteins

C. Conditionally Essential Amino Acids

n Sometimes a nonessential amino acid becomes essential under
special circumstances.

n For example, the body normally uses the essential amino acid
phenylalanine to make tyrosine (a nonessential amino acid).
But if the diet fails to supply enough phenylalanine, or if the
body cannot make the conversion for some reason (as
happens in the inherited disease phenylketonuria), then
tyrosine becomes a conditionally essential amino acid.

CHS 214 – Madawi Aldhwayan 9

 The Chemist’s View of Proteins

Proteins
n Cells link amino acids end-to-end in a variety of sequences to
form thousands of different proteins.

n A peptide bond unites each amino acid to the next.

CHS 214 – Madawi Aldhwayan 10

 The Chemist’s View of Proteins

Amino Acid Chains:

n Condensation reactions connect amino acids, Two amino acids
bonded together form a dipeptide.

n A third amino acid can be added to the chain to form a

tripeptide. As additional amino acids join the chain, a
polypeptide is formed.
n Most proteins are a few dozen to several hundred amino acids
long.

CHS 214 – Madawi Aldhwayan 11

 The Chemist’s View of Proteins

Amino Acid Sequences

n amino acid sequences within proteins vary.
n The 20 amino acids can be linked together in a variety of
sequences

CHS 214 – Madawi Aldhwayan 12

 The Chemist’s View of Proteins

Protein shapes:
n Polypeptide chains twist into a variety of complex, tangled
shapes, depending on their amino acid sequences. The unique
side group of each amino acid gives it characteristics that
attract it to, or repel it from, the surrounding fluids and other
amino acids.

n Hydrophobic
n Hydrophilic

CHS 214 – Madawi Aldhwayan 13

 The Chemist’s View of Proteins

Protein Functions
n The unique shapes of proteins enable them to perform their
various tasks in the body.
n Some form hollow balls that can carry and store materials
within them, and some, such as those of tendons, are more
than ten times as long as they are wide, forming strong, rod
like structures.
n Some polypeptides are functioning proteins just as they are;
others need to associate with other polypeptides.
n Some proteins require minerals to activate them. One
molecule of hemoglobin made of four associated polypeptide
chains, each holding the mineral iron.
CHS 214 – Madawi Aldhwayan 14
 The Chemist’s View of Proteins

Protein Denaturation
n When proteins are subjected to heat, acid, or other conditions
that disturb their stability, they undergo denaturation

n They uncoil and lose their shapes and also lose their ability to
function.
n Denaturation is irreversible.
n the hardening of an egg when it is cooked,
n the curdling of milk when acid is added,
n the stiffening of egg whites when they are whipped

CHS 214 – Madawi Aldhwayan 15

 Digestion and Absorption of Protein

Digestion and Absorption of Protein

n Proteins in foods do not become body proteins directly. Instead,
they supply the amino acids from which the body makes its own
proteins.

Food Polypeptide Tripeptide Dipeptide Amino acids

CHS 214 – Madawi Aldhwayan 16

Digestion and Absorption of Protein

Protein Digestion
In the Stomach:
n The major event in the stomach is the partial breakdown
(hydrolysis) of proteins.
n Hydrochloric acid uncoils (denatures) each protein’s tangled
strands so that digestive enzymes can attack the peptide
bonds.
n The hydrochloric acid also converts the inactive form of the
enzyme pepsinogen to its active form, pepsin.
n Pepsin cleaves proteins—large polypeptides—into smaller
polypeptides and some amino acids.

CHS 214 – Madawi Aldhwayan 17

 Digestion and Absorption of Protein

In the Small Intestine:

n When polypeptides enter the small intestine, several
pancreatic and intestinal proteases hydrolyze them further
into short peptide chains, tripeptides, dipeptides, and amino
acids.
n Then peptidase enzymes on the membrane surfaces of the
intestinal cells split most of the dipeptides and tripeptides into
single amino acids.
n Only a few peptides escape digestion and enter the blood
intact.

CHS 214 – Madawi Aldhwayan 18

Digestion and Absorption of Protein

Protein Absorption
n A number of specific carriers transport amino acids (and some
dipeptides and tripeptides) into the intestinal cells.

n Once inside the intestinal cells, amino acids may be used for
energy or to synthesize needed compounds. Amino acids that
are not used by the intestinal cells are transported across the
cell membrane into the surrounding fluid where they enter the
capillaries on their way to the liver.

CHS 214 – Madawi Aldhwayan 19

Digestion and Absorption of Protein

CHS 214 – Madawi Aldhwayan 20

CHS 214 – Madawi Aldhwayan 21
 Proteins in the Body

Sequencing Errors
n The sequence of amino acids in each protein determines its
shape and function. If a genetic error alters the amino acid
sequence of a protein, or if a mistake is made in copying the
sequence, an altered protein will result, sometimes with
dramatic consequences.

n Hemoglobin offers one example of such a genetic variation.

CHS 214 – Madawi Aldhwayan 22

CHS 214 – Madawi Aldhwayan 23
Proteins in the Body

CHS 214 – Madawi Aldhwayan 24

 2. Roles of Proteins

As Building Materials for Growth and Maintenance

n proteins form the building blocks of muscles, blood, and most
body structures.

n To build a bone or a tooth, cells first lay down a matrix of the

protein collagen and then fill it with crystals of calcium,
phosphorus, magnesium, fluoride, and other minerals.

n Collagen also provides the material of ligaments and tendons

and the strengthening glue between the cells of the artery
walls that enables the arteries to withstand the pressure of the
blood with each heartbeat.
CHS 214 – Madawi Aldhwayan 25
 2. Roles of Proteins

n Proteins are also needed for replacing dead or damaged cells.

The life span of a skin cell is only about 30 days. As old skin
cells are shed, new cells made largely of protein grow from
underneath to replace them.

n Muscle cells make new proteins to grow larger and stronger in

response to exercise.

n Cells of the GI tract are replaced every few days.

CHS 214 – Madawi Aldhwayan 26

 2. Roles of Proteins

As Enzymes
n Some proteins act as enzymes, eg. digestive enzymes

n Enzymes not only break down substances, but they also build
substances (such as bone) and transform one substance into
another (amino acids into glucose).

CHS 214 – Madawi Aldhwayan 27

 2. Roles of Proteins

As Hormones
n The body’s many hormones are messenger molecules, and
some hormones are proteins.

n The blood carries the hormones from these glands to their

target tissues, where they elicit the appropriate responses to
restore and maintain normal conditions.

n The hormone insulin provides an example

CHS 214 – Madawi Aldhwayan 28

CHS 214 – Madawi Aldhwayan 29
 2. Roles of Proteins

As Regulators of Fluid Balance

n Blood proteins such as albumin and globulin help to maintain
the body’s fluid balance. (proteins attract water from leaking
to the interstitial space )

n the body’s fluids are contained inside the cells (intracellular) or

outside the cells (extracellular).

n Extracellular fluids, can be found either in the spaces between

the cells (interstitial) or within the blood vessels
(intravascular).
n The fluid within the intravascular spaces is called plasma
(essentially blood without its red blood cells).
CHS 214 – Madawi Aldhwayan 30
 2. Roles of Proteins

n Fluids can flow freely between these compartments, but being

large, proteins cannot. Proteins are trapped primarily within
the cells and to a lesser extent in the plasma.

n The exchange of materials between the blood and the cells

takes place across the capillary walls, which allow the passage
of fluids and a variety of materials.

n Some plasma proteins leak out of the capillaries into the

interstitial fluid between the cells, but can reenter the system
via the lymphatic system.

CHS 214 – Madawi Aldhwayan 31

CHS 214 – Madawi Aldhwayan 32
 2. Roles of Proteins

n If plasma proteins enter the interstitial spaces faster than they

can be cleared, fluid accumulates (because plasma proteins
attract water) and causes swelling. Swelling due to an excess
of interstitial fluid is known as edema.
n The protein-related causes of edema include:
• Excessive protein losses caused by kidney disease or
large wounds (such as extensive burns)
• Inadequate protein synthesis caused by liver disease
• Inadequate dietary intake of protein
n Whatever the cause of edema, the result is the same: a
diminished capacity to deliver nutrients and oxygen to the cells
and to remove wastes from them. As a consequence, cells fail
to function adequately.

CHS 214 – Madawi Aldhwayan 33

 2. Roles of Proteins

As Acid-Base Regulators
n Proteins also help to maintain the balance between acids and
bases within the body fluids.

n In an acid solution, hydrogen ions (H+) abound; the more

hydrogen ions, the more concentrated the acid. Proteins,
which have negative charges on their surfaces, attract
hydrogen ions, which have positive charges.

CHS 214 – Madawi Aldhwayan 34

 2. Roles of Proteins

n By accepting and releasing hydrogen ions, proteins maintain

the acid-base balance of the blood and body fluids.

n The blood’s acid-base balance is tightly controlled. The

extremes of acidosis and alkalosis lead to coma and death,
largely because they denature working proteins.

n example, denatured hemoglobin loses its capacity to carry

oxygen.

CHS 214 – Madawi Aldhwayan 35

 2. Roles of Proteins

As Transporters
n Some proteins move about in the body fluids, carrying
nutrients and other molecules.

n The protein hemoglobin carries oxygen from the lungs to the

cells.

n The lipoproteins transport lipids around the body. Special

transport proteins carry vitamins and minerals.

CHS 214 – Madawi Aldhwayan 36

 2. Roles of Proteins

n Each transport protein is specific for a certain compound or

group of related compounds.

n A membrane-bound transport protein helps to maintain the

sodium and potassium concentrations in the fluids inside and
outside cells. The balance of these two minerals is critical to
nerve transmissions and muscle contractions; imbalances can
cause irregular heartbeats, muscular weakness, kidney failure,
and even death.

CHS 214 – Madawi Aldhwayan 37

 2. Roles of Proteins

As Antibodies
n Proteins also defend the body against disease.

n When the body detects these invading antigens, it

manufactures antibodies, giant protein molecules designed
specifically to combat them.

n The antibodies work efficiently that in a normal, healthy

individual, most diseases never have a chance to get started.
Without sufficient protein, the body cannot maintain its army
of antibodies to resist infectious diseases.

CHS 214 – Madawi Aldhwayan 38

 2. Roles of Proteins

As a Source of Energy and Glucose

n Without energy, cells die; without glucose, the brain and
nervous system falter.

n Proteins can be sacrificed to provide energy and glucose during

times of starvation or insufficient carbohydrate intake.

n The body will break down its tissue proteins to make amino
acids available for energy or glucose production.

n protein can maintain blood glucose levels, but at the expense

of losing lean body tissue.
CHS 214 – Madawi Aldhwayan 39
 2. Roles of Proteins

Other Roles
n Proteins form integral parts of most body structures such as
skin, muscles, and bones.

n They also participate in blood clotting and vision. When a

tissue is injured, a rapid chain of events leads to the
production of fibrin, a stringy, insoluble mass of protein fibers
that forms a solid clot from liquid blood. Later, more slowly,
the protein collagen forms a scar to replace the clot and
permanently heal the wound.

CHS 214 – Madawi Aldhwayan 40

 2. Roles of Proteins

n The light-sensitive pigments in the cells of the eye’s retina are

molecules of the protein opsin.

n Opsin responds to light by changing its shape, thus initiating

the nerve impulses that convey the sense of sight to the brain.

CHS 214 – Madawi Aldhwayan 41

CHS 214 – Madawi Aldhwayan 42
 A Preview of Protein Metabolism

Protein Turnover and the Amino Acid Pool

n Within each cell, proteins are continually being made and
broken down, a process known as protein turnover.

n When proteins break down, they free amino acids. These

amino acids mix with amino acids from dietary protein to form
an “amino acid pool” within the cells and circulating blood.

CHS 214 – Madawi Aldhwayan 43

 A Preview of Protein Metabolism

n The rate of protein degradation and the amount of protein

intake may vary, but the pattern of amino acids within the pool
remains fairly constant.

n Regardless of their source, any of these amino acids can be

used to make body proteins or other nitrogen-containing
compounds, or they can be stripped of their nitrogen and used
for energy.

CHS 214 – Madawi Aldhwayan 44

 A Preview of Protein Metabolism

Nitrogen Balance
n Protein turnover and nitrogen balance go hand in hand.
n In healthy adults, protein synthesis balances with degradation,
and protein intake from food balances with nitrogen excretion
in the urine, feces, and sweat.
n When nitrogen intake equals nitrogen output, the person is in
nitrogen equilibrium, or zero nitrogen balance.
n Researchers use nitrogen balance studies to estimate protein
requirements. If the body synthesizes more than it degrades
and adds protein, nitrogen status becomes positive.

CHS 214 – Madawi Aldhwayan 45

 A Preview of Protein Metabolism

n Nitrogen status is positive in growing infants, children,

adolescents, pregnant women, and people recovering from
protein deficiency or illness; their nitrogen intake exceeds their
nitrogen output. They are retaining protein in new tissues as
they add blood, bone, skin, and muscle cells to their bodies.

n If the body degrades more than it synthesizes and loses

protein, nitrogen status becomes negative. Nitrogen status is
negative in people who are starving or suffering other severe
stresses such as burns, injuries, infections, and fever; their
nitrogen output exceeds their nitrogen intake. During these
times, the body loses nitrogen as it breaks down muscle and
other body proteins for energy.
CHS 214 – Madawi Aldhwayan 46
 A Preview of Protein Metabolism

Using Amino Acids to Make Proteins or Nonessential Amino

Acids
n Cells can assemble amino acids into the proteins they need to
do their work. If a particular nonessential amino acid is not
readily available, cells can make it from another amino acid. If
an essential amino acid is missing, the body may break down
some of its own proteins to obtain it.

n Using Amino Acids to Make Other Compounds Cells can also

use amino acids to make other compounds. For example, the
amino acid tyrosine is used to make the neurotransmitters
norepinephrine and epinephrine, which relay nervous system
messages throughout the body.
CHS 214 – Madawi Aldhwayan 47
 A Preview of Protein Metabolism

n Tyrosine can also be made into the pigment melanin, which is

responsible for brown hair, eye, and skin color, or into the
hormone thyroxin, which helps to regulate the metabolic rate.

n For another example, the amino acid tryptophan serves as a

precursor for the vitamin niacin and for serotonin, a
neurotransmitter important in sleep regulation, appetite
control, and sensory perception.

CHS 214 – Madawi Aldhwayan 48

 A Preview of Protein Metabolism

Using Amino Acids for Energy and Glucose

n when glucose or fatty acids are limited, cells are forced to use
amino acids for energy and glucose.

n The body does not make a specialized storage form of protein

as it does for carbohydrate and fat. protein in the body is
available only from the working and structural components of
the tissues.

n When the need arises, the body breaks down its tissue
proteins and uses their amino acids for energy or glucose.
n Thus, over time, energy deprivation always causes wasting of
lean body tissue as well as fat loss.
CHS 214 – Madawi Aldhwayan 49
 A Preview of Protein Metabolism

Deaminating Amino Acids

n When amino acids are broken down (used for energy), they are first
deaminated—stripped of their nitrogen- containing amino groups.

n Deamination produces ammonia, which the cells release into the

bloodstream. The liver picks up the ammonia, converts it into urea (a
less toxic compound), and returns the urea to the blood.

n The production of urea increases as dietary protein increases, until

production hits its maximum rate at intakes approaching 250 grams
per day.

n The kidneys filter urea out of the blood; thus the amino nitrogen
ends up in the urine.

CHS 214 – Madawi Aldhwayan 50

 A Preview of Protein Metabolism

Using Amino Acids to Make Fat

n Amino acids may be used to make fat when energy and
protein intakes exceed needs and carbohydrate intake is
adequate.

n The amino acids are deaminated, the nitrogen is excreted, and

the remaining carbon fragments are converted to fat and
stored for later use.

n In this way, protein-rich foods can contribute to weight gain.

CHS 214 – Madawi Aldhwayan 51

A Preview of Protein Metabolism

CHS 214 – Madawi Aldhwayan 52

 Protein in Foods

Protein Quality
n The protein quality of the diet determines how well children
grow and how well adults maintain their health.
n high-quality proteins provide enough of all the essential amino
acids needed to support the body’s work, and low quality
proteins don’t.

n Two factors influence protein quality—the protein’s

digestibility and its amino acid composition.

CHS 214 – Madawi Aldhwayan 53

 Protein in Foods

Digestibility:
n proteins must be digested before they can provide amino
acids. Protein digestibility depends on such factors as the
protein’s source and the other foods eaten with it.

n The digestibility of most animal proteins is high (90 to 99

percent); plant proteins are less digestible (70 to 90 percent
for most, but over 90 percent for soy and legumes).

CHS 214 – Madawi Aldhwayan 54

 Protein in Foods

Amino Acid Composition

n To make proteins, a cell must have all the needed amino acids
available simultaneously. The liver can produce any
nonessential amino acid that may be in short supply so that
the cells can continue linking amino acids into protein strands.

n If an essential amino acid is missing, though, a cell must

dismantle its own proteins to obtain it. Therefore, to prevent
protein breakdown, dietary protein must supply at least the
nine essential amino acids plus enough nitrogen- containing
amino groups and energy for the synthesis of the others.

CHS 214 – Madawi Aldhwayan 55

 Protein in Foods

n If the diet supplies too little of any essential amino acid,

protein synthesis will be limited.

n The body makes whole proteins only; if one amino acid is

missing, the others cannot form a “partial” protein. An
essential amino acid supplied in less than the amount needed
to support protein synthesis is called a limiting amino acid.

CHS 214 – Madawi Aldhwayan 56

 Protein in Foods

Reference Protein
n The quality of a food protein is determined by comparing its
amino acid composition with the essential amino acid
requirements of preschool age children.

n Such a standard is called a reference protein.

n The rationale behind using the requirements of this age group

is that if a protein will effectively support a young child’s
growth and development, then it will meet or exceed the
requirements of older children and adults.

CHS 214 – Madawi Aldhwayan 57

 Protein in Foods

High-Quality Proteins
n a high-quality protein contains all the essential amino acids in
relatively the same amounts and proportions that human beings
require; it may or may not contain all the nonessential amino acids.

n Proteins that are low in an essential amino acid cannot, by

themselves, support protein synthesis. Generally, foods derived from
animals (meat, fish, poultry, cheese, eggs, yogurt, and milk) provide
high-quality proteins,

n Proteins from plants (vegetables, nuts, seeds, grains, and legumes)

have more diverse amino acid patterns and tend to be limiting in one
or more essential amino acids.
n Some plant proteins are notoriously low quality (for example, corn
protein). A few others are high quality (for example, soy protein).
CHS 214 – Madawi Aldhwayan 58
 Protein in Foods

Complementary Proteins
n many vegetarians improve the quality of proteins in their diets
by combining plant-protein foods that have different but
complementary amino acid patterns.

n This strategy yields complementary proteins that together

contain all the essential amino acids in quantities sufficient to
support health.

n The protein quality of the combination is greater than for

either food alone.

CHS 214 – Madawi Aldhwayan 59

 Protein in Foods

n Many people believe that combining plant proteins at every

meal is critical to protein nutrition. For most healthy
vegetarians, it is not necessary to balance amino acids at each
meal if protein intake is varied and energy intake is sufficient.

n Vegetarians can receive all the amino acids they need over the
course of a day by eating a variety of whole grains, legumes,
seeds, nuts, and vegetables.

n Protein deficiency will develop, however, when fruits and

certain vegetables make up the core of the diet, severely
limiting both the quantity and quality of protein.
CHS 214 – Madawi Aldhwayan 60
Protein in Foods

CHS 214 – Madawi Aldhwayan 61

Protein in Foods

CHS 214 – Madawi Aldhwayan 62