PROTEIN

organic compounds that have large molecules composed of one or more long chains of amino acids and are an essential part
of all living organisms, especially as structural components of body tissues such as muscle, hair, etc., and as enzymes and
antibodies.

During peptide bonds- hydrogen and oxygen atom is lost and dehydration synthesis reaction occur.

WHAT IS PROTEIN?
Proteins are;

• bioorganic molecules
• Macromolecule
• Biomolecules
• Proteins are involved in most of the body's functions
and life processes
Ex: Body Defenses and Metabolism
Proteins differ based on the sequence of amino acid which is
determined by the DNA.

SYNTHESIS AND BREAKOWN OF PROTEIN

A dehydration reaction occurs when two monomers bond together through the loss of a water molecule.
Polymers are disassembled to monomers by hydrolysis, a reaction that is essentially the reverse of the dehydration
reaction.

WHY IS PROTEIN CONSIDERED A MACROMOLECULE?

1. Molecules are made up of 2 or more atoms that are covalently bonded.

• Protein as a macro/ biomolecule • Made up of different atoms that are covalently bonded.

The following atoms bond to form amino acid which is the monomer of protein:

• Carbon • Oxygen
• Hydrogen • Nitrogen

2. Macromolecules are large molecules

› Proteins are large molecules that are made up of subunits of amino acids.

4. Carbon bonds form the framework of biomolecules.

› Carbon bonds form the framework of proteins.

Below is an example of a primary protein structure formed by a chain of amino acids bonded together by peptide links.

• A linear chain of amino acids is called polypeptide.

• Proteins are often called polypeptides because they are composed of amino acids
held together by peptide bonds.

• A macromolecule protein contains at least 1 long polypeptide.

The chains of amino acids fold into a particular form during its synthesis. The shape of a particular protein determines its
function.

A. Hemoglobin is a protein shaped to hold oxygen for transport through the bloodstream.

B. A group of proteins called enzymes are shaped to fit and react with specific molecules.

• Enzymes have different shapes specific for the digestion of a certain biomolecule.

• Amylase is an enzyme that aids in the digestion of starch.

STRUCTURES OF THE PROTEIN

• Primary Structure • Tertiary Structure

• Secondary Structure • Quaternary Structure

Combination of either pure helix or pure beta or a combination of both.

DENATURING OF PROTEIN

Alteration of the protein’s shape and thus functions through the use of:

✓ Heat ✓ Salts
✓ Acids ✓ Mechanical Agitation
✓ Bases
Primary structure is unchanged by denaturing.

A linear chain of amino acids is called polypeptide.

• Protein contains at least 1 long polypeptide.

• Proteins are classified by the number of amino acids in a chain

➢ Dipeptides have 2 amino acids.
➢ Tripeptides have 3 amino acids.
➢ Peptides have less than 20 amino acids.
➢ Oligopeptides when there are 20-30 amino acids.
➢ Proteins have more than 50 amino acid
Typically, 100 to 10,000 amino acids linked together
HOW ARE PROTEINS FORMED?
• Peptide bonds link amino acids.

• Proteins are also formed when the acid group (COOH)

of one amino acid joins with the amine group (NH2) of a
second amino acid.

• Same with other biomolecules:

➢ Formed through condensation reaction

(release of H20).
➢ Broken through hydrolysis (addition of H20).

PROTEIN DIGESTION

Mouth and salivary glands.

Mechanical digestion of protein begins with chewing, tearing,

and mixing food with salivary juices to form a bolus.

= Bolus

Stomach

Hydrochloric acid denatures protein and activates pepsinogen to

form pepsin. Pepsin breaks the polypeptide chain into smaller
polypeptides.

= Denatured protein = Polypeptide chain

Small intestine and pancreas

Enzymes from the pancreas enter the small intestine and

continue to cleave peptide bonds, resulting in dipeptides,
tripeptides, and single amino acids.

= Tripeptides and single amino acids

Small intestine lining

Tripeptidases and dipeptidases on the surface of the small

intestinal cells finish the digestion to yield [ingle amino acids,
which can then be absorbed.

= Single amino acids

ESSENTIAL, NONESSENTIAL, AND CONDITIONAL AMINO ACID:

1. Essential amino acids- are amino acids that cannot be made by the body. As a result, they must come from
food.
 - The 9 essential amino acids are: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine,
tryptophan, and valine

2. Nonessential amino acids-Nonessential means that our bodies can produce the amino acid, even if we do
not get it from the food we eat.

- Nonessential amino acids include alanine, arginine, asparagine, aspartic acid, cysteine, glutamic acid,
glutamine, glycine, proline, serine, and tyrosine.

3. Conditionally essential - Needs to be consumed as it cannot be synthesized due to illness or lack of

necessary precursors

- Conditional amino acids are usually not essential, except in times of illness and stress.

- Example: premature infants who lack sufficient enzymes needed to create arginine.

• L-arginine is an amino acid that helps the body to build proteins

AMINO ACID METABOLISM

• Liver metabolizes amino acids, • Most amino acids are sent into the • Protein turnover- the continual
depending on bodily needs. blood to be picked up and used by degradation and synthesizing of
the cells. Amino acid pool is limited proteins
but has many uses.

DEAMINATION
• When the amino acid pool reaches capacity, the amino
acids are broken down to their component parts for other
uses.
• First deamination must occur.
• Carbon-containing remnants are:
➢ Converted to glucose, if they are glucogenic amino
acids, through gluconeogenesis.
➢ Converted to fatty acids and stored as triglycerides in
adipose tissue

QUICK REVIEW

• During digestion •The amino acid pool acts as a reservoir for protein
- Proteins are broken down to amino acid with the help of synthesis.
➢ Gastric juices •Surplus amino acids are:
➢ Enzymes in the stomach and small intestine - Deaminated
➢ Enzymes from the pancreas and small intestine lining ➢ Used for glucose or energy.
➢ Stored as fat.
• Limited supply of amino acids exists in the amino acid ➢ Nitrogen is converted to urea and excreted in
pool. urine.
 FUNCTIONS OF PROTEIN
1. Building Body Constituents 2. Hormones
• All cells contain protein. • Protein as a hormone function in cell signaling or
• All body cells break down, and protein is needed for communication within the cell.
continual repair and rebuilding • It regulates body functions including metabolic rate
though the thyroid hormone and blood glucose regulation
through the hormones insulin and glucagon.
3. Maintaining Fluid Balance Immune Function (Protection from illness)
• Fluid flows from the capillary bed into the • Both White blood cells and antibodies protects the body
extracellular space (spaces between cells) to nourish against infection.
the cells. - White blood cells are part of the body's immune system.
• Protein stays in the intravascular compartment or They help the body fight infection and other diseases. All
within the blood vessels because they are too large to white blood cells require amino acids in order to sustain
move through the vessel walls. normal function.
• The function of protein in the capillaries is to attract • Antibodies
fluid back into the intravascular compartment. - antibodies are proteins, and are therefore made up of
• If there is inadequate protein, there is nothing to amino acids
attract the fluid that leaves the intravascular
compartment.
- Edema may take place.
4. Enzymes 5. Energy
• Enzymes are proteins that help speed up • Provides little energy to the body except in prolonged
metabolism, or the chemical reactions in our bodies. exercise.
They build some substances and break others down. • Can be a source of glucose as a result of gluconeogenesis.

6. Acid-Base Balance 7. Can be Converted to Glucose

• Proteins help regulate acid-base balance in the • Maintains the normal blood sugar level as a source of
blood. energy needed by the brain and the red blood cells to
- The pH measures the acidity or alkalinity function.
➢ pH of 7 = neutral - The brain uses 19% of the body's energy even at
➢ pH<7 = acidic rest.
➢ pH>7 = alkaline or base • Amino acids can be converted to glucose through the
• The body must keep balance of the acidity and process called gluconeogenesis.
alkalinity in order to function properly. • Carbohydrate is the primary source of energy needed for
- Even a slight change in this balance can affect the the body to function.
many organs. • A person may not be able to consume carbohydrates but
- Each time there's a change in the acid-base still be able to function. This is because of the process
balance, the body automatically pushes the blood pH called gluconeogenesis.
level back to normal. • Gluconeogenesis (GNG) results in the production of
• Proteins pump ions in and out of the cells to regulate glucose from non-carbohydrate carbon substrates like
the pH. protein.
• Proteins serve as buffers. The compounds that • The purpose of gluconeogenesis is to maintain the
maintain the acidity within a narrow range. blood glucose level during fasting
WHICH CONDITION CONTRAINDICATES THE HIGH INTAKE OF PROTEIN?
• Diet high in protein is not indicated to people with preexisting kidney disease.

• This is because of the excess nitrogen found in the amino acids that make up proteins. Damaged kidneys have to work
harder to get rid of the extra nitrogen and waste products of protein metabolism.

BEST SOURCES OF PROTEIN

• Proteins are abundant in • 3 oz serving of cooked meat, poultry, or fish
- Dairy foods - Provides 21-25 grams of protein
- Meats - About 7 g/oz
- Poultry - About the size of a deck of cards
- Meat alternatives such as dried beans, peanut butter, - Adequate amount for one meal
nuts, and soy

EATING TOO MUCH PROTEIN EATING TOO LITTLE PROTEIN

➢ Risk of heart disease ➢ Protein-energy malnutrition (PEM)
➢ Risk of kidney stones ✓ Protein is used for energy rather than its other functions in the body.
➢ Risk of calcium loss from bones ✓ Other important nutrients are in short supply.
➢ Risk of colon cancer ➢ Without adequate protein
➢ Displacement of other nutrient-rich, ✓ Cells lining the GI tract are not sufficiently replaced as they slough
disease preventing foods off.
✓ Digestive function is inhibited.
✓ Absorption of food is reduced.
✓ Intestinal bacteria get into the blood and causes septicemia.
➢ Immune system is compromised due to malnutrition and cannot fight
infection
TYPES OF PEM
1. KWASHIORKOR 3. MARASMUS 4. MARASMIC KWASHIORKOR
2. • Chronic deficiency in kilocalories and
• Severe protein deficiency Manifestations:
protein
➢ Generally, result of a diet high in • "skin and bones" appearance
grains and deficient in protein. • Little or no subcutaneous fat
• Reduced brain growth ➢ Have edema in legs and arms.
• Symptoms range from ➢ Have a "skin and bones" appearance.
➢Edema in legs, feet, and stomach • Results from a severe deficiency in
➢ With treatment the edema subsides,
➢Muscle tone and strength diminish. kilocalories
➢Frail, emaciated appearance. and appearance becomes more like
➢Hair is brittle and easy ta pull out. someone with marasmus.
➢Appear pale, sad, and apathetic. ➢Weakened and appear apathetic.
➢Prone to infection, rapid heart rate, ➢Many cannot stand without
excess fluid in lungs, pneumonia, support.
septicemia, and water and ➢Look old.
electrolyte imbalances ➢Hair is thin, dry, and lacks sheen.
➢Body temperature and blood
pressure are low.
➢Prone to dehydration, infections,
and unnecessary blood clotting.