Carbohydrates

Carbohydrates, or carbs, are sugar molecules. They are the primary energy source for
human, and almost all other living organisms. Along with proteins and fats, carbohydrates
are one of three main nutrients found in foods and drinks. These molecules contain
carbon, hydrogen, and oxygen atoms. Carbohydrates play an important role in the human
body. They help control blood glucose and insulin metabolism, participate in cholesterol
and triglyceride metabolism, and help with fermentation.

Types of Carbohydrates

Monosaccharides

- Carbohydrates consisting of one sugar molecule. Monosaccharides can be further

classified based on the number of carbon atoms. These are trioses, tetroses,
pentoses, hexoses, and heptoses.
- Break down quickly in the body.
- Provide a quick burst of energy or a “sugar rush.”

Examples of Monosaccharides

1. Glucose - is one the simplest forms of sugars. It is the main type of sugar in the
blood and is the major source of energy for the body's cells. Glucose comes from
the foods we eat, or the body can make it from other substances. Glucose is
carried to the cells through the bloodstream. Several hormones, including insulin,
control glucose levels in the blood.
- It is the most common and abundant monosaccharides present in all
carbohydrates.

2. Fructose - is also known as “fruit sugar” because it primarily occurs naturally in

many fruits. It also occurs naturally in other plant foods such as honey, sugar
beets, sugar cane and vegetables.

3. Galactose - It is similar to glucose in its structure, differing only in the position of

one hydroxyl group. This difference, however, gives galactose different chemical
and biochemical properties to glucose.

- It is mainly found in milk and other dairy products because it is a precursor for
milk sugar.
Linear Form

Disaccharides – any substance that is composed of two molecules of simple sugars

(monosaccharides) linked to each other. Disaccharides are crystalline water-soluble
compounds.

- Also known as double sugar

- Joined by glycosidic linkage – a covalent bond formed between two
monosaccharides.

Examples of Disaccharides:

1. Sucrose
- Glucose + Fructose = Sucrose
- also known as cane sugar, occurs in sugar cane stems, sweet fruits, and certain
storage roots. it consists of a glucose and a fructose molecule combined together.
2. Lactose
– glucose + Galactose = Lactose
- also known as milk sugar, is commonly found in milk. it is found in milk of all
mammals, including humans and even in some similar fluids. it is formed from
glucose and galactose combined together.

3. Maltose
- Glucose + Glucose = Maltose
- also known as malt sugar, is present in malted cereals and sprouting grains. it is
formed from the partial digestion of starch and is a combination of two glucose
molecules.
Condensation - is a chemical reaction whereby two simple molecules are joined together to
form a larger molecule with the removal of one molecule of water.

Hydrolysis - when a disaccharide is treated with a suitable enzyme, it breaks down to

form monosaccharides.

Oligosaccharides - contain between 3 and 10 single sugar residues and are not relatively
abundant in the diet when compared to other more common carbohydrates like those in
the disaccharide category. Common oligosaccharides include raffinose, stachyose, and
verbascose.

Polysaccharides – are the most complex carbohydrates and its examples include starch
and cellulose. There are other substances which are slightly modified carbohydrates.
Serves as storage and structure material for cells or the whole organism.

Cellulose - It’s a structural carbohydrate that is found in the cell wall of every plant cell
helping plants to remain stiff and upright. Humans cannot digest cellulose, but it is
important in the diet as fiber.

Starches - are found in many of the foods we eat such as potatoes and corn. Starches are
also found in grains such as wheat and rice.

Glycogen - extra glucose molecules that the body doesn’t immediately need for energy are
stored as polysaccharides called glycogen either in the liver or in skeletal muscles.
 Proteins
Proteins

 Large, complex molecules that play many critical roles in the body.
 Most of the work in cells and are required for the structure, function, and
regulation of the body’s tissues and organs.
 Made up of hundreds or thousands of smaller units or called amino acids.
 Your body uses them to make new proteins, such as muscle and bone.
 Energy source
 20 different types of amino acids that can be combined to make a protein.

 Amino acids are coded by combinations of three DNA building blocks (nucleotides).
 Components: carbon, hydrogen, oxygen, sulfur, nitrogen, and sometimes
phosphorus.

Functions of Protein

1. Metabolism
 Enzymes
 Biological Catalysts- speed up chemical reactions
 Digestive enzymes aid in hydrolysis
 Lipase
  Amylase
 Lactase
 Protease
2. Molecular Biology
 Polymerase
 Ligase
3. Structural Support
 Keratin- hair and nails
 Collagen- supports ligaments, tendons, and skin
 Silk- cocoons and spider webs
4. Transport
 transport molecules in blood
 Hemoglobin - transports oxeygen in blood
5. Defense
 Antibodies - combat bacteria and viruses
6. Regulation
 Hormones - intercellular messengers that influence metabolism
 Insulin - regulates the amount of glucose in the blood and in cellls
 Human Growth Hormone - its presence determines the height of an individual
 Receptor Proteins - built into the membranes of nerve cells
7. Motion
 Muscle Contraction- Actin and Myosin makes up muscle fibers
 Motor Protein within the cell- allow cell components to move from place to
place

The Chemical Structure of Protein

Proteins are made up of hundreds or thousands

of smaller units or monomers called amino acids,
which are attached to one another in long
chains. There are 20 different types of amino
acids that can be combined to make a protein.
In chemistry, an amino acid is an organic compound that contains both an amino (-NH2)
and carboxylic acid (-COOH) functional group, hence the name amino acid. The sequence of
amino acids determines each protein’s unique 3-dimensional structure and its specific
function. Amino acids are coded by combinations of three DNA building blocks
(nucleotides), determined by the sequence of genes. The difference in the R-group is what
determines the unique properties of each amino acid.

 The primary structure is comprised of a linear chain of amino acids.

 The secondary structure contains regions
of amino acid chains that are stabilized by
hydrogen bonds from the polypeptide
backbone. These hydrogen bonds create
alpha-helix and beta-pleated sheets of the
secondary structure.
 The three-dimensional shape of a protein, its
tertiary structure, is determined by the
interactions of side chains from the polypeptide
backbone.
 The quaternary structure also influences the three-
dimensional shape of the protein and is
formed through the side-chain
interactions between two or more
polypeptides.

In a β pleated sheet, two or more

segments of a polypeptide chain line up
next to each other, forming a sheet-like
structure held together by hydrogen
bonds. The hydrogen bonds form between
carbonyl and amino groups of backbone,
while the R groups extend above and below
the plane of the sheet. The strands of a β
pleated sheet may be parallel, pointing in
the same direction (meaning that their
Amine group and Carboxyl group match up), or antiparallel, pointing in opposite directions
(meaning that the Amine group of one strand is positioned next to the carboxyl group of
the other)

In an α helix, the carbonyl (C=O) of one amino acid is hydrogen bonded to the
amino H (N-H) of an amino acid that is four down the chain. This pattern of bonding pulls
the polypeptide chain into a helical structure that resembles a curled ribbon,

Sources of Protein

1. Lean meats 6. Nuts

 2. Poultry 7. Legumes and beans
3. Fish and seafoods 8. Grain and cereal-based products
4. Eggs
5. Dairy products

Examples of Protein

There is a total of seven different protein types under which all proteins fall.
These are:

1. Antibodies- Antibodies are specialized proteins that defend the body against
antigens or foreign invaders. The purpose of this in our immune system is for
defense against pathogens. Their ability to travel through the bloodstream
enables them to be utilized by the immune system to identify and defend against
bacteria, viruses, and other foreign intruders in blood. One way antibodies
counteract antigens is by immobilizing them so that they can be destroyed by
white blood cells.
2. Contactile Proteins- Responsible for muscle contraction and movement.
3. Enzymatic Proteins- The catalysts of all metabolic reactions, enable an organism to
build up the chemical substances necessary for life—proteins, nucleic acids,
carbohydrates, and lipids—to convert them into other substances, and to degrade
them.
 Life without enzymes is not possible
4. Hormonal- are messenger proteins that help coordinate certain bodily functions.
5. Structural (collagen)- The most common example of a structural protein is collagen
which is found in the bones, cells and skin. collagen is an exaple of fibrous protein.
 Structural proteins are also found in cells. They are used to provide an
internal structure to the cell (the cytoskeleton) and are sometimes
involved in cell movement. Structural proteins are especially important in
larger cells.
6. Storage- Storage proteins reserve amino acids for the body until ready for use.
 Ferritin a storage protein that stores iron.
7. Transport- Transport proteins are carrier proteins that move molecules from one
place to another in the body.

Additional Informations

Proteins serve crucial roles in human biochemistry. The major role is to provide
the body's building blocks. They are the precursors of several biologically relevant
molecules. Therefore either the excess or deficiency of protein can lead to disease result
in nervous system defects, metabolic problems, organ failure, and even death.

 The most severe form of protein deficiency is called kwashiorkor; Anorexia

Nervosa.
 A dysfunctional protein can lead to a variety of medical conditions and, often,
death.
  Dysfunctional proteins can lead to childhood obesity, breakdown of the retina
leading to blindness, hearing loss, and type 2 diabetes.

The National Academy of Medicine recommends that adults get a minimum of 0.8 grams of
protein for every kilogram of body weight per day, or just over 7 grams for every 20
pounds of body weight.

 For a 140-pound person, that means about 50 grams of protein each day.
 For a 200-pound person, that means about 70 grams of protein each day.

The National Academy of Medicine also sets a wide range for acceptable protein intake—
anywhere from 10% to 35% of calories each day. Beyond that, there’s relatively little solid
information on the ideal amount of protein in the diet or the healthiest target for calories
contributed by protein. In an analysis conducted at Harvard among more than 130,000
men and women who were followed for up to 32 years, the percentage of calories from
total protein intake was not related to overall mortality or to specific causes of death.
However, the source of protein was important