BIO 001

Dr. A. M. Oloyede
Department of Cell Biology and Genetics
University of Lagos
Biological Molecules

• Carbohydrates

• Lipids

• Proteins

• Nucleic acids
Carbohydrates
• Formula (CH2O)n, where n is the number
of carbons in the molecule.

• the ratio of carbon to hydrogen to oxygen is 1:2:1 in

carbohydrate molecules.

• Because they contain many carbon-hydrogen (C—H) bonds,

which release energy when they are broken, carbohydrates
are well suited for energy storage.
Classification

Monosaccharides

Disaccharides

Polysaccharides
 Monosaccharides
• The simple sugars
• Contain as few as three carbon atoms, but those that play
the central role in energy storage have six
• The empirical formula of six-carbon sugars is: C6H12O6, or
(CH2O)6
• Six-carbon sugars can exist in a straight-chain form, but in
an aqueous environment they almost always form rings.
• The most important of these for energy storage is
glucose a six-carbon sugar which has seven energy
storing C—H bonds.
Disaccharides
• Are “double sugars,” two monosaccharides
joined by a covalent bond – glycosidic bond
• They often play a role in the transport of
sugars

• Condensation—remove water
• Hydrolysis ----Add water
 Polysaccharides
• Macromolecules made up of monosaccharide subunits.
• Starch is a polysaccharide used by plants to store energy.
• It consists entirely of glucose molecules, linked one after another in
long chains.
• Cellulose is a polysaccharide that serves as a structural building
material in plants. It too consists entirely of glucose molecules
linked together into chains, and special enzymes are required to
break the links.
 Sugar Isomers
• Alternative forms, of glucose.

• Even though isomers have the same empirical formula, their atoms are
arranged in different ways; i.e, their three-dimensional structures are
different.

• These structural differences often account for substantial functional

differences between the isomers.

• Glucose and fructose, for example, are structural isomers.

 Isomers and stereoisomers

Glucose, fructose, and galactose are isomers with the empirical formula C6H12O6.
A structural isomer of glucose, such as fructose, has identical chemical groups
bonded to different carbon atoms, while a stereoisomer of glucose, such as
galactose, has identical chemical groups bonded to the same carbon atoms but in
different orientations.
The structural differences among sugar

isomers can confer substantial

functional differences upon the

molecules
 Transport disaccharide
• In humans, the glucose that circulates in the blood does so
as a simple monosaccharide.
• In plants and many other organisms, however, glucose is
converted into a transport form before it is moved from
place to place within the organism.
• In such a form it is less readily metabolized (used for energy)
during transport. Transport forms of sugars are commonly
made by linking two monosaccharides together to form a
disaccharide
Glucose forms transport disaccharides with itself and many other monosaccharides,
including fructose and galactose.

When glucose forms a disaccharide with its structural isomer, fructose, the resulting
disaccharide is sucrose, or table sugar

Sucrose is the form in which most plants transport glucose and the sugar that most
humans (and other animals) eat. Sugarcane is rich in sucrose, and so are sugar beets.

When glucose is linked to its stereoisomer, galactose, the resulting disaccharide is

lactose, or milk sugar.

Many mammals supply energy to their young in the form of lactose.

Adults have greatly reduced levels of lactase, the enzyme required to cleave lactose into
its two monosaccharide components, and thus cannot metabolize lactose as
efficiently. Most of the energy that is channeled into lactose production is therefore
reserved for their offspring
 Storage polysaccharide
• Organisms store the metabolic energy contained in monosaccharides
by converting them into disaccharides, such as maltose

• These insoluble polysaccharides are long polymers of

monosaccharides formed by dehydration synthesis.

• Plant polysaccharides formed from glucose are called starches. Plants

store starch as granules within chloroplasts and other organelles.
Because glucose is a key metabolic fuel, the stored starch provides a
reservoir of energy available for future needs. Energy for cellular
work can be retrieved by hydrolyzing the links that bind the glucose
subunits together. Amylose)
The animal version of starch is
glycogen. Like amylopectin, glycogen
is an insoluble polysaccharide
containing branched amylose chains.
Some disaccharides are used to transport glucose from one part of an organism’s
body to another; one example is sucrose (a), which is found in sugarcane. Other
disaccharides, such as maltose in grain (b), are used for storage.
Nonfattening Sweets
•Imagine a kind of table sugar that looks, tastes, and
cooks like the real thing, but has no calories or harmful
side effects.
•Most sugars are “right-handed” molecules, in that the
hydroxyl group that binds a critical carbon atom is on the
right side.
•However, “left-handed” sugars, in which the hydroxyl
group is on the left side, can be made readily in the
laboratory.
Left-handed sugars are called levo-, or 1-sugars. They do not
occur in nature except for trace amounts in red algae, snail eggs,
and seaweed. Because they pass through the body without
being used, they can let diet-conscious sweet-lovers have their
cake and eat it, too. Nor will they contribute to tooth
decay because bacteria cannot metabolize them, either.
Starches are glucose polymers. Most starches are

branched and some are cross-linked. The branching

and cross-linking render the polymer insoluble and

protect it from degradation.

Structural Carbohydrates

• Structural carbohydrates are chains of sugars that are not easily

digested. They include cellulose in plants and chitin in arthropods

and fungi.
 Cellulose
• For two glucose molecules to link together, the glucose subunits must be the
same form.

• Glucose can form a ring in two ways, with the hydroxyl group attached to the
carbon where the ring closes being locked into place either below or above the
plane of the ring. If below, it is called the alpha form, and if above, the beta
form.

• All of the glucose subunits of the starch chain are alpha-glucose.

When a chain of glucose molecules consists of all beta-glucose subunits, a polysaccharide with very different
properties results. This structural polysaccharide is cellulose, the chief component of plant cell walls
 Cellulose contd.

• Cellulose is chemically similar to amylose, with one important difference: the

starch-degrading enzymes that occur in most organisms cannot break the bond
between two beta-glucose sugars.

• This is not because the bond is stronger, but rather because its cleavage requires
an enzyme most organisms lack.

• Because cellulose cannot be broken down readily, it works well as a biological

structural material and occurs widely in this role in plants.
Those few animals able to break
down cellulose find it a rich
source of energy. Certain
vertebrates, such as cows, can
digest cellulose by means of
bacteria and protists they harbor
in their intestines which provide
the necessary enzymes.
 Chitin
• The structural building material in insects,
many fungi, and certain other organisms is
called chitin

• Chitin is a modified form of cellulose with a

nitrogen group added to the glucose units.
When cross-linked by proteins, it forms a
tough, resistant surface material that serves as
the hard exoskeleton of arthropods such as
insects and crustaceans

• Few organisms are able to digest chitin.

Lipids
• Diverse group of compounds that are largely
nonpolar in nature. This is because they are
hydrocarbons that include mostly nonpolar
carbon–carbon or carbon–hydrogen bonds.

• Non-polar molecules are hydrophobic (“water

fearing”), or insoluble in water.
 Functions
• Cells store energy for long-term use in the form of fats (numerious
C-H bonds)

• Provide insulation from the environment for plants and animals

• Building blocks of many hormones

• Important constituent of all cellular membranes

• Many vitamins are fat soluble

Lipids include fats, oils, waxes, phospholipids, and steroids

 Fats and Oils
• Two main components—glycerol and fatty acids.
• Glycerol is an organic compound (alcohol) with three
carbons, five hydrogens, and three hydroxyl (OH) groups.
• Fatty acids have a long chain of hydrocarbons to which a
carboxyl group is attached, hence the name “fatty acid.”
• The number of carbons in the fatty acid may range from 4
to 36; most common are those containing 12–18 carbons.
• In a fat molecule, the fatty acids are attached to each of
the three carbons of the glycerol molecule with an ester
bond through an oxygen atom
 Fatty acids may be saturated or unsaturated

• In a fatty acid chain, if there are only single bonds between neighboring
carbons in the hydrocarbon chain, the fatty acid is said to be saturated.
Saturated fatty acids are saturated with hydrogen; in other words, the
number of hydrogen atoms attached to the carbon skeleton is maximized.
E.g Stearic acid.

• When the hydrocarbon chain contains a double bond, the fatty acid is said
to be unsaturated. E. g Oleic acid
 Stearic acid is a common saturated fatty acid

Oleic acid is a common unsaturated fatty acid

Most unsaturated fats are liquid at room temperature and are called oils.
If there is one double bond in the molecule, then it is known as a monounsaturated fat (e.g., olive oil), and

if there is more than one double bond, then it is known as a polyunsaturated fat (e.g., canola oil).
Animal fats with stearic acid and palmitic acid (common in meat) and the fat with butyric
acid (common in butter) are examples of saturated fats.

Mammals store fats in specialized cells called adipocytes

In plants, fat or oil is stored in many seeds and is used as a source of energy during
seedling development.
Unsaturated fats or oils are usually of plant origin and contain cis unsaturated fatty acids.

Cis and trans indicate the configuration of the molecule around the double bond.

If hydrogens are present in the same plane, it is referred to as a cis fat;

if the hydrogen atoms are on two different planes, it is referred to as a trans fat.

The cis double bond causes a bend or a “kink” that prevents the fatty acids from packing
tightly, keeping them liquid at room temperature Olive oil, corn oil, canola oil, and cod
liver oil are examples of unsaturated fats. Unsaturated fats help to lower blood
cholesterol levels whereas saturated fats contribute to plaque formation in the arteries.
 Trans Fats
• In the food industry, oils are artificially hydrogenated to make
them semi-solid and of a consistency desirable for many
processed food products. During this hydrogenation process,
double bonds of the cis- conformation in the hydrocarbon chain
may be converted to double bonds in the trans- conformation.
• Margarine, some types of peanut butter, are examples of
artificially hydrogenated trans fats.
• Recent studies have shown that an increase in trans fats in the
human diet may lead to an increase in levels of low-density
lipoproteins (LDL), or “bad” cholesterol, which in turn may lead
to plaque deposition in the arteries, resulting in heart disease.
 Fats as Food
• When an organism consumes excess carbohydrate, it is converted into
starch, glycogen, or fats and reserved for future use.
• The reason that many humans gain weight as they grow older is that
the amount of energy they need decreases with age, while their intake
of food does not. Thus, an increasing proportion of the carbohydrate
they ingest is available to be converted into fat.
• A diet rich in fats is one of several factors that contribute to heart
disease, particularly to atherosclerosis, a condition in which deposits
of fatty tissue called plaque adhere to the lining of blood vessels,
blocking the flow of blood. Fragments of plaque, breaking off from a
deposit, are a major cause of strokes.
Essential Fatty Acids
• Fatty acids required but not synthesized by the human body.
Consequently, they have to be supplemented through
ingestion via the diet.

Omega-3 fatty acids

Omega-6 fatty acid

These are polyunsaturated fatty acids

Waxes
• Covers the feathers of some aquatic birds and
the leaf surfaces of some plants.

• Waxes are made up of long fatty acid chains

esterified to long-chain alcohols.
Phospholipids
• Major constituents of the plasma membrane, the outermost
layer of animal cells.
• Like fats, they are composed of fatty acid chains attached to a
glycerol or sphingosine backbone.
• Instead of three fatty acids attached as in triglycerides,
however, there are two fatty acids forming diacylglycerol, and
the third carbon of the glycerol backbone is occupied by a
modified phosphate group
 Note pls
A phosphate group alone attached to a diacylglycerol does not
qualify as a phospholipid; it is phosphatidate (diacylglycerol 3-
phosphate), the precursor of phospholipids. The phosphate group is
modified by an alcohol.

• Phosphatidylcholine and phosphatidylserine are two important

phospholipids that are found in plasma membranes
Phospholipids contd.
Phospholipids contd.
(a) At an oil-water interface, phospholipid molecules will orient so that their polar (hydrophilic) heads are
in the polar medium, water, and their nonpolar (hydrophobic) tails are in the nonpolar medium, oil.

(b) When surrounded by water, phospholipid molecules arrange themselves into two layers with their
heads extending outward and their tails inward.
Phospholipids are responsible for the dynamic
nature of the plasma membrane. If a drop of
phospholipids is placed in water, it
spontaneously forms a structure known as a
micelle, where the hydrophilic phosphate heads
face the outside and the fatty acids face the
interior of this structure.
Steroids
• Have a fused ring structure. Although they do not resemble
the other lipids, they are grouped with them because they
are also hydrophobic and insoluble in water.

• All steroids have four linked carbon rings and several of

them, like cholesterol, have a short tail.

• Many steroids also have the –OH functional group, which

puts them in the alcohol classification (sterols)
Steroids such as cholesterol and cortisol are composed of four fused hydrocarbon rings.
Cholesterol
• Cholesterol is the most common steroid. Cholesterol is mainly
synthesized in the liver and is the precursor to many steroid
hormones such as testosterone and estradiol, which are secreted by
the gonads and endocrine glands.

• It is also the precursor to Vitamin D.

• Cholesterol is also the precursor of bile salts, which help in the

emulsification of fats and their subsequent absorption by cells.
 PROTEINS

• Are one of the most abundant organic molecules in living

systems
• They have most diverse range of functions of all
macromolecules.
• Proteins may be structural, regulatory, contractile, or protective;
they may serve in transport, storage, or membranes; or they may
be toxins or enzymes.
• Each cell in a living system may contain thousands of proteins,
each with a unique function.
• Their structures, like their functions, vary greatly.
• They are all polymers of amino acids, arranged in a linear
sequence.
Types and Functions of Proteins
 Shapes
• Proteins have different shapes and molecular weights; some
proteins are globular in shape whereas others are fibrous in nature.
For example, haemoglobin is a globular protein, but collagen, found
in our skin, is a fibrous protein.
• Protein shape is critical to its function, and this shape is maintained
by many different types of chemical bonds.
• Changes in temperature, pH, and exposure to chemicals may lead to
permanent changes in the shape of the protein, leading to loss of
function, known as denaturation.
• All proteins are made up of different arrangements of the same 20
types of amino acids.
 Amino acids
• Amino acids are the monomers that make up proteins. Each amino acid has the
same fundamental structure, which consists of a central carbon atom, also
known as the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl
group (COOH), and to a hydrogen atom. Every amino acid also has another
atom or group of atoms bonded to the central atom known as the R group
A peptide bond forms when the —NH2 end of one amino acid joins to the —COOH end of another.
Because of the partial double-bond nature of peptide bonds, the resulting peptide chain cannot rotate
freely around these bonds.
 The classes of amino acids
• Each amino acid has the same chemical backbone, but differs in the side, or R group it
possesses.
• Six of the amino acids are nonpolar because they have —CH2 or —CH3 in their R
groups. Two of the six are bulkier because they contain ring structures, which classifies
them also as aromatic. (NA) Alanine, Valine, Leucine, Isoleucine.(A) Phenylalanine,
Tryptophan
• Another six are polar because they have oxygen or just hydrogen in their R groups;
these amino acids, which are uncharged, differ from one another in how polar they
are. (N/A) Glycine, Serine, Threonine, Asparagine, Glutamine (A) Tyrosine
• Five other amino acids are polar and, because they have a terminal acid or base in
their R group, are capable of ionizing to a charged form. Glutamic acid, Aspartic acid,
Histidine, Lysine and Arginine.
• The remaining three have special chemical properties that allow them to help form
links between protein chains or kinks in proteins. Proline, Methionine and Cysteine.
 Protein Structure
• Primary - The unique sequence of amino acids in a polypeptide chain is
its primary structure

• Secondary - The local folding of the polypeptide in some regions gives

rise to the secondary structure of the protein. The most common are the
α-helix and β-pleated sheet structures

• Tertiary - The unique three-dimensional structure of a polypeptide is its

tertiary structure

• Quaternary -In nature, some proteins are formed from several

polypeptides, also known as subunits, and the interaction of these
subunits forms the quaternary structure.
 Primary structure
• This sequence is determined by the nucleotide sequence of the gene that

encodes the protein. Because the R groups that distinguish the various amino

acids play no role in the peptide backbone of proteins, a protein can consist

of any sequence of amino acids. Thus, a protein containing 100 amino acids

could form any of 20 *100 different amino acid sequences. This is an

important property of proteins because it permits great diversity.

 Secondary Structure
The amino acid side groups are not the only portions of proteins that
form hydrogen bonds. The —COOH and —NH2 groups of the main
chain also form good hydrogen bonds. Two patterns of H bonding
occur. In one, hydrogen bonds form along a single chain, linking one
amino acid to another farther down the chain. This tends to pull the
chain into a coil called an alpha (α) helix. In the other pattern,
hydrogen bonds occur across two chains, linking the amino acids in
one chain to those in the other. Often, many parallel chains are linked,
forming a pleated, sheetlike structure called a β-pleated sheet. The
folding of the amino acid chain by hydrogen bonding into these
characteristic coils and pleats is called a protein’s secondary structure.
 Tertiary Structure
The final folded shape of a globular protein, which positions the various motifs and
folds nonpolar side groups into the interior, is called a protein’s tertiary structure. A
protein is driven into its tertiary structure by hydrophobic interactions with water. The
final folding of a protein is determined by its primary structure—by the chemical nature
of its side groups. Many proteins can be fully unfolded (“denatured”) and will
spontaneously refold back into their characteristic shape.

The stability of a protein, once it has folded into its 3-D shape, is strongly influenced by
how well its interior fits together. When two nonpolar chains in the interior are in very
close proximity, they experience a form of molecular attraction called van der Waal’s
forces.
 Quaternary Structure
• When two or more polypeptide chains associate to form a functional
protein, the individual chains are referred to as subunits of the protein. The
subunits need not be the same. Hemoglobin, for example, is a protein
composed of two α-chain subunits and two β-chain subunits. A protein’s
subunit arrangement is called its quaternary structure. In proteins
composed of subunits, the interfaces where the subunits contact one
another are often nonpolar, and play a key role in transmitting information
between the subunits about individual subunit activities. A change in the
identity of one of these amino acids can have profound effects.
• Sickle cell haemoglobin is a mutation that alters the identity of a single
amino acid at the corner of the β subunit from polar glutamate to nonpolar
valine. Putting a nonpolar amino acid on the surface creates a “sticky patch”
that causes one hemoglobin molecule to stick to another, forming long
nonfunctional chains and leading to the cell sickling characteristic of this
hereditary disorder.
 Denaturation
• Each protein has its own unique sequence and shape that are held together by chemical
interactions. If the protein is subject to changes in temperature, pH, or exposure to
chemicals, the protein structure may change, losing its shape without losing its primary
sequence in what is known as denaturation. Denaturation is often reversible because
the primary structure of the polypeptide is conserved in the process if the denaturing
agent is removed, allowing the protein to resume its function. Sometimes denaturation
is irreversible, leading to loss of function.
• One example of irreversible protein denaturation is when an egg is fried. The albumin
protein in the liquid egg white is denatured when placed in a hot pan.
• Not all proteins are denatured at high temperatures; for instance, bacteria that survive
in hot springs have proteins that function at temperatures close to boiling.
• The stomach is also very acidic, has a low pH, and denatures proteins as part of the
digestion process; however, the digestive enzymes of the stomach retain their activity
under these conditions.
 Protein Folding
Protein folding is critical to its function. often they receive assistance in the

folding process from protein helpers known as chaperones (or chaperonins)

that associate with the target protein during the folding process. They act

by preventing aggregation of polypeptides that make up the complete

protein structure, and they disassociate from the protein once the target

protein is folded.
Thank you