Biochemistry: Protein

CAPE Biology (Part I)

Introduction

Much of the body is made of protein, and these proteins take on a myriad of forms. They
represent cell signaling receptors, signaling molecules, structural members, enzymes,
intracellular trafficking components, extracellular matrix scaffolds, ion pumps, ion channels,
oxygen and CO​2 transporters (hemoglobin). That is not even the complete list! There is
protein in bones (collagen), muscles, and tendons; the hemoglobin that transports oxygen;
and enzymes that catalyze all biochemical reactions. Protein is also used for growth and
repair. Amid all these necessary functions, proteins also hold the potential to serve as a
metabolic fuel source.

There are four levels of protein structures namely:

1. Primary structure
2. Secondary structure
3. Tertiary structure
4. Quaternary structure

Proteins (a polymer) are macromolecules composed of amino acid subunits (the monomers
). These amino acids are covalently attached to one another to form long linear chains
called polypeptides, which then fold into a specific three-dimensional shape. Sometimes
these folded polypeptide chains are functional by themselves. Other times they combine
with additional polypeptide chains to form the final protein structure. Sometimes
non-polypeptide groups are also required in the final protein. For instance, the blood protein
hemogobin is made up of four polypeptide chains, each of which also contains a heme
molecule, which is ring structure with an iron atom in its center.

Proteins have different shapes and molecular weights, depending on the amino acid
sequence. For example, hemoglobin is a globular protein, which means it folds into a
compact globe-like structure, but collagen, found in our skin, is a fibrous protein, which
means it folds into a long extended fiber-like chain. You probably look similar to your family
members because you share similar proteins, but you look different from strangers because
the proteins in your eyes, hair, and the rest of your body are different.
Primary structure of protein

The primary structure is the linear sequence of amino acids in a polypeptide chain held by
`covalent peptide bonds. The correct sequence of amino acids allows proteins to be folded
in a specific way so that they will effectively carry out their biological functions. Thus, any
changes in the sequence of an amino acid within the polypeptide chain will disrupt the
normal function of the protein.

Secondary structure of protein

The polypeptide chain of the primary structure can coil or fold to form two different
secondary structures. Coiling results into alpha helix and folding results into beta- pleated
sheet. The coiling and folding of the secondary structure is due exclusively to hydrogen
bonding within the polypeptide chain backbone and not by side chains/R groups.
Alpha helix

The shape of the helix is maintained by regularly spaced hydrogen bonds that are formed
between a hydrogen atom of one amino group and oxygen from the carboxylic group of
another amino acid. Hydrogen bonding may take place between amino acids higher up in
the polypeptide chain and those lower down in the polypeptide chain. The alpha helix is the
most common component of protein secondary structures.

Beta- Pleated Sheet

In contrast to the alpha helical structure, beta-pleated sheet consists of two or more
polypeptides chains connected to each other through hydrogen bonding. These
polypeptide chains may run parallel or antiparallel. Hydrogen bonding occurs between a
hydrogen atom in the amino group of one of the polypeptide chain and oxygen in the
carboxylic group of another polypeptide chain.

Tertiary structure of protein

1
The tertiary structure describes how regions of secondary structure (alpha helices,
beta-pleated sheets) fold to forma three dimensional shape. An alpha helix may fold in a
globular compact manner to yield the tertiary structure of a protein. It is at the tertiary level
that proteins begin to carry out their biological functions. For example, forming enzymes and
hormones. The stabilization of the tertiary structure results mostly from interactions between
side chains. Whereas, the secondary structure is stabilized only by hydrogen bonding within
the polypeptide chain backbone. The tertiary structure is stabilized by a variety of bonds.

Types of Bonds Stabilizing Tertiary Structure of Protein

1. Hydrogen bonds
2. Ionic bonds
3. Strong Covalent bonds
4. Hydrophobic interactions

Summary of the types of bonds that stabilize the tertiary structure.

1. Hydrogen Bond

● Hydrogen bonds may form between hydrogen from one amino group and O from the
carboxylic group of another amino acid within the backbone of the polypeptide chain.
 ● Hydrogen atoms can also be formed between a hydrogen atom of one side chain
and O from another side chain.

Fig 5: Hydrogen bond between side chains/R groups of two amino acids (serine).

2. Ionic Bonds

● Ionic bonding occurs between the positively and negatively charged "R" groups that
come in close contact with one another. An amino acid containing an acidic carboxyl
group( COOH ) on its side chain may form ionic bond with a basic amino acid
that contain NH2 in its side chain .
● Some amino acids (such as aspartic acid and glutamic acid) contain an extra -COOH
group. Some amino acids (such as lysine) contain an extra -NH2 group. You can get
a transfer of a hydrogen ion from the -COOH to the -NH2. The carboxylic group will
then form COO- (negatively charged ion) . The hydrogen will associates with the
amino group to form NH3+ ( positively charged ion).
 Fig 6 : Ionic reaction between R groups of the amino acid lysine and aspartic acid .

3. Covalent Bond

The R-group of the amino acid cysteine contains a sulphur atom. This sulphur atom will of
covalently form bond with another sulphur atom in the same polypeptide chain or in
another polypeptide chain (inter chain). Two hydrogen atoms are removed to form the
disulphide bond.
 Fig 7 : Formation of a disulphide bond between the amino acids cysteine

Fig 8: Disulphide bond between amino acids cysteine in a polypeptide chain.

4. Hydrophobic Interactions

Hydrophobic interactions are formed between R groups/side chains that are non-polar and
hydrophobic. Some amino acids have side chains/R groups that are non-polar and
hydrophobic. These side chains cannot hydrogen bond with water. Therefore, they are
buried in the interior of the protein as they shield themselves from the water. Conversely,
polar/hydrophilic amino acid side-chains tend to on the surface of a protein where they are
exposed to the aqueous environment. Hydrophobic interactions greatly contribute to the
folding and shaping of a protein. However, the tertiary structure depends on its primary
structure, as the bonds holding the tertiary structure together can only be formed if the
correct amino acids are at specific points along a polypeptide chain.
 ●

Fig 9: Folding of polypeptide chain due to hydrophobic reaction

Quaternary structure

The quaternary structure is formed from the combination of two or more polypeptide
chains which are chemically bonded to each other. The quaternary structure may be
associated with non-protein groups as in the case of haemoglobin that consists of an haem
group. The quaternary structure of protein may also be divided in globular or fibrous
proteins. For, example haemoglobin is a globular protein and collagen is a fibrous protein
with quaternary structure.
Fig 11: The quaternary structure of haemoglobin . Each alpha and beta polypepide chain
is about 140 amino acids long.
 Fig 12: The quaternary structure of collagen molecule (tropocollagen).

Three helical polypeptide chains that are supercoiled to form a ropelike structure. Each helix
consists of a 1000 amino acid.

Functions of proteins

Antibodies

Antibodies are specialized proteins involved in ​defending the body from antigens (foreign
invaders). They can travel through the blood stream and are utilized by the immune system
to identify and defend against bacteria, viruses, and other foreign intruders. One way
antibodies counteract antigens is by immobilizing them so that they can be destroyed by
white blood cells.

Contractile proteins

Contractile proteins are responsible for movement​. Examples include actin and myosin.
These proteins are involved in muscle contraction and movement.

Enzymes

Enzymes are proteins that facilitate ​biochemical reactions​. They are often referred to as
catalysts because they speed up chemical reactions. Examples include the enzymes
lactase and pepsin. Lactase breaks down the sugar lactose found in milk. Pepsin is a
digestive enzyme that works in the stomach to break down proteins in food.
 Enzyme reaction​: A catabolic enzyme reaction showing the substrate matching the exact
shape of the active site.

Hormonal proteins

Hormonal proteins are messenger proteins which help to ​coordinate certain bodily
activities​. Examples include insulin, oxytocin, and somatotropin. Insulin regulates glucose
metabolism by controlling the blood-sugar concentration. Oxytocin stimulates contractions
in females during childbirth. Somatotropin is a growth hormone that stimulates protein
production in muscle cells.

Structural proteins

Structural proteins are fibrous and stringy and ​provide support​. Examples include keratin,
collagen, and elastin. Keratins strengthen protective coverings such as hair, quills, feathers,
horns, and beaks. Collagens and elastin provide support for connective tissues such as
tendons and ligaments.

Storage proteins

Storage proteins ​store amino acids​. Examples include ovalbumin and casein. Ovalbumin
is found in egg whites and casein is a milk-based protein.

Transport proteins

Transport proteins are ​carrier proteins which move molecules from one place to another
around the body. Examples include hemoglobin and cytochromes. Hemoglobin transports
oxygen through the blood. Cytochromes operate in the electron transport chain as electron
carrier proteins.

Denaturation of protein

Any agent that breaks the bonds within the three dimensional structure of the protein will
allow the shape of the protein to be changed and prevent them from carrying out their
biological functions. For example, when enzymes become denatured they lose their active
site and are unable to bind to a substrate. Some factors that cause proteins to become
denatured are: heat, acids, alkalis, inorganic chemicals, organic chemicals and mechanical
force. The primary structure (which is the amino acid sequence) of a protein remains
unaffected by denaturation. Only the bonds that maintain the secondary (backbone
conformation), tertiary (overall 3 dimensional arrangement) and quaternary (subunit
interaction) are destroyed.

Reversing Denaturation
It is often possible to reverse denaturation because the primary structure of the polypeptide,
the covalent bonds holding the amino acids in their correct sequence, is intact. Once the
denaturing agent is removed, the original interactions between amino acids return the
protein to its original conformation and it can resume its function.

However, denaturation can be irreversible in extreme situations, like frying an egg. The heat
from a pan denatures the albumin protein in the liquid egg white and it becomes insoluble.
The protein in meat also denatures and becomes firm when cooked.

Denaturing a protein is occasionally irreversible: (Top) The protein albumin in raw and
cooked egg white. (Bottom) A paperclip analogy visualizes the process: when cross-linked,
 paperclips (‘amino acids’) no longer move freely; their structure is rearranged and
‘denatured’.

Chaperone proteins (or chaperonins ) are helper proteins that provide favorable conditions
for protein folding to take place. The chaperonins clump around the forming protein and
prevent other polypeptide chains from aggregating. Once the target protein folds, the
chaperonins disassociate.

Classifications of protein

Classification of Protein based on their Three Dimensional Shape.

Proteins can be divided into two general types on the basis of their tertiary structure:

1. Fibrous proteins
2. Globular Proteins

1. Fibrous Protein

Fibrous proteins are elongated rope–like structures, with the polypeptide chains arranged in
long strands. In fibrous proteins, the polypeptide backbone does not fold globularly upon
itself.

Summary of Fibrous Protein

● They look like long filament rope.

● They are parallel polypeptide chains cross-linked in long fibres or sheets.
● They are usually insoluble in water.
● Their roles include protection and support, forming connective tissue, bone
matrices, and muscle fiber.
● They are physically tough which allow them to carry out their structural function.

2. Globular Proteins

The polypeptide chains are tightly folded to form a spherical shape (ball-like shape.
Globular proteins are folded so that the hydrophobic groups are on the inside of the
molecule and the hydrophilic groups face outwards in the aqueous environment, making
these proteins soluble in water. Globular proteins include enzymes, antibodies and
hormones.

Summary of Globular Proteins

● They have complex tertiary and sometimes quaternary structures.

● They are folded into spherical (globular) shapes.
● They are usually soluble as hydrophobic side chains in centre of structure.
● They play a roles in metabolic reactions such as digestion and respiration. .

​Components of phospholipids

Phospholipids are major components of the plasma membrane, the outermost layer of
animal cells. Like fats, they are composed of fatty acid chains attached to a glycerol
backbone. Unlike triglycerides, which have three fatty acids, phospholipids have two fatty
acids that help form a diacylglycerol. The third carbon of the glycerol backbone is also
occupied by a modified phosphate group However, just a phosphate group attached to a
diacylglycerol does not qualify as a phospholipid. This would be considered a phosphatidate
(diacylglycerol 3-phosphate), the precursor to phospholipids. To qualify as a phospholipid,
the phosphate group should be modified by an alcohol. Phosphatidylcholine and
phosphatidylserine are examples of two important phospholipids that are found in plasma
membranes.
 Phospholipid Molecule

A phospholipid is a molecule with two fatty acids and a modified phosphate group attached
to a glycerol backbone. The phosphate may be modified by the addition of charged or polar
chemical groups. Two chemical groups that may modify the phosphate, choline and serine,
are shown here. Both choline and serine attach to the phosphate group at the position
labeled R via the hydroxyl group indicated in green.

Components of phospholipids
● Two fatty acids chains( tails)
● One glycerol
● Phosphoric acid
● The third hydroxyl group of glycerol combines with phosphoric acid to form a polar
phosphate head .
● The phosphate head is polar and hydrophilic ( water loving)
● The fatty acids tails are non-polar and are hydrophobic (water hating) .
● Phospholipids are amphipathic having a hydrophobic (non-polar) tail and
hydrophilic (polar) head.

A phospholipid molecule
 Model of a saturated fatty acid chain

Grey for CARBON = C, Blue for Hydrogen = H and Red for Oxygen = O
 Model of a unsaturated fatty acid chain

Model of hydrophilic and hydrophobic regions of a phospholipid

Micelle

When mixed with water, phospholipids form droplet spheres with the hydrophilic heads
facing

the water and the hydrophobic tails facing each other. This is called a micelle.
hydrophilic (polar) head of the phospholipid extends outward in water while

hydrophobic (non-polar) tails is shielded away from water.

Double layered phospholipid bilayer. This traps a compartment of water in the middle

separated from the external water by the hydrophobic sphere. This naturally-occurring
structure

is called a liposome, and is similar to a membrane surrounding a cell.

 Phosopolipid bilayer of cell membrane. A hydrophilic head and a hydrophobic tail,

allow the phospholipid to form a bilayer when immersed in water. This effect takes place
due to

the fact that water clings to the hydrophilic head ( the hydrophilic heads facing the water)
and the

hydrophobic tails facing each other as they shield themselves away from water.
Fig 10 : Tertiary structure of a globular protein (myoglobin)
Further Classification of Protein

Proteins can also be classified as simple or conjugated.

Simple Protein

● The simple proteins are those which are made of amino acid units only, joined by
peptide bond. For example, albumin and serum

Conjugated Protein

● Conjugated proteins are composed of simple proteins combined with a

non-proteinous substance. The non-proteinous substance is called prosthetic group
or cofactor. For example, haemoglobin in which haem is the prosthetic group.

Structure of phospholipids and their role in cell membrane

The fluidity of the phospholipid bilayer is greatly due to its unique structure. Each
phospholipid consists of a polar group head which is connected by a glycerol to two fatty
acid chains. Sometimes the two fatty acid chains differ in that one is saturated and one in
unsaturated, depending on the environment where the species is acclimated. . In the
unsaturated fatty acid, a cis-bond ( carbon double bond ) is present creating a "kink" in the
tail. This does not allow the phospholipids to pack too closely together when placed in a
cold environment. For the phospholipid bilayer to do this, more phospholipids must be
created and cholesterol must be present. In extremely cold temperatures, more unsaturated
fatty acid tailed phospholipids are created to prevent the bilayer from losing its much
needed fluidity
Kink in fatty acid tail of the phospholipid which is made up of unsaturated fatty acids
(cis-fatty acids).

● The fluidity talked about above allows the membrane to move and curve in the
presence of tension. This bending and curving motion is called the curvature of the
membrane. Plasma membranes have curvature due to constant changes of pressure
from the environment, as well as changes inside the cell. By having the ability to
"mold" to different types of strains, plasma membranes are able to stay intact and
play their important roles in the cell.

● Due to the fact that the inner components of the bilayer are hydrophobic, the
membrane is impermeable to most biological molecules and water-soluble
molecules. This means that most molecules cannot get through the membrane and
into the cell. Water, oxygen, and carbon dioxide and lipid soluble molecules can
easily diffuse through the membrane unassisted.

● The fluidity of the cell membrane allows amphipathic membrane protein to span the
cell membrane to take across substances that could not otherwise enter or leave
the cell. These include polar and charged molecules such as amino acids,
glucose and ions such as sodium, chloride, calcium and potassium. These
substances are essential to the survival of the organism.
 The phospholipid bilayer provides fluidity to the cell membrane which allows proteins to
transport substances into and out of the cell .

Functions of phospholipids

Phospholipid

1. Separates the inside of the cell from its external surrounding.

2. Are major component of cell membrane/plasma membrane.
3. Provides fluidity to the cell membrane.
4. Are selectively permeable thus allowing only some substances to move in and out of
the cell.
5. Shields the cell from any surrounding harm while also maintaining a steady
fluctuation of nutrients and water into and out of the cell.

Other lipids

Other Lipids

1. Cholesterol
2. Waxes
3. Steroids
4. Terpenes
5. Glycolipids
1. Cholesterol

Cholesterol is an amphipathic molecule, meaning, like phospholipids, it contains a

hydrophilic and a hydrophobic portion. Cholesterol's hydroxyl (OH) group aligns with
the phosphate heads of the phospholipids. The remaining portion of it tucks into the
fatty acid portion of the membrane. Because of the way cholesterol is shaped, part of
the steroid ring (the four hydrocarbon rings in between the hydroxyl group and the
hydrocarbon "tail") is closely attracted to part of the fatty acid chain on the nearest
phospholipid. This helps slightly immobilize the outer surface of the membrane and
make it less soluble to very small water-soluble molecules that could otherwise pass
through more easily. Without cholesterol, cell membranes would be too fluid, not firm
enough, and too permeable to some molecules. In other words, it keeps the
membrane from turning to mush.

○ Cholesterol helps maintain the fluidity of cell membranes.

○ Cholesterol adds firmness and integrity to the plasma membrane and
prevents it from becoming overly fluid, it also helps maintain its fluidity. At the
high concentrations it is found in our cell's plasma membranes (close to 50
percent, molecule for molecule) cholesterol helps separate the phospholipids
so that the fatty acid chains do not come together and cyrstallize. Therefore,
cholesterol helps prevent extremes - whether too fluid, or too firm - in the
consistency of the cell membrane.
○ Cholesterol helps secure important proteins in the membrane. The plasma
membrane contains many proteins that perform important functions like
channeling or pumping substances into and out of the cell, attaching to other
cells, forming borders to keep other proteins in one specific part of the cell,
communicating with nearby cells, or responding to endocrine hormones from
far-away cells. Because certain proteins' size or shape requires a thicker
phospholipid bed to sit in, and because certain proteins need to stick together
to function properly, the fluidity of the cell membrane, where the molecules
are constantly moving randomly, could pose a problem. Fortunately, the
plasma membrane contains many lipid rafts where proteins are secured. A
lipid raft contains high concentrations of cholesterol and sphingolipids - a type
of phospholipid - containing longer and more saturated fatty acid tails. By
stabilizing certain proteins together in lipid rafts, cholesterol is important to
helping these proteins maintain their function.
2.

Fig 10: Chloseterol is a component of the cell memebrane; in helping to maintain

structure and function.

3. Waxes

A second group of neutral lipids that are of physiological importance, though they
are a minor component of biological systems, are waxes. Essentially, waxes consist
of a long-chain fatty acid linked through an ester oxygen to a long-chain . These
molecules are completely water-insoluble and generally solid at biological
temperatures. Their strongly hydrophobic nature allows them to function as water
repellents on the leaves of some plants, on feathers, and on the cuticles of certain
insects. Waxes also serve as energy-storage substances in (microscopic aquatic
plants and animals) and in higher members of the aquatic food chain. Plankton
apparently use the biosynthesis of waxes to adjust their buoyant density and thus
their depth in the ocean. It has been suggested that a major source of petroleum
found in deep-sea sediments originates from the deposition of wax-rich dead
plankton over vast periods of time. Whales and many fishes also store large
quantities of waxes.
 4. Steroids

A steroid compound (referred to as a sterol) has as its foundation a set of four

hydrocarbon rings bonded to a variety of other atoms and molecules. Although both
plants and animals synthesize sterols, the type that makes the most important
contribution to human structure and function is cholesterol, which is synthesized by
the liver in humans and animals and is also present in most animal-based foods.
Like other lipids, cholesterol’s hydrocarbons make it hydrophobic; however, it has a
polar hydroxyl head that is hydrophilic. Cholesterol is an important component of bile
acids, compounds that help emulsify dietary fats. In fact, the word root chole- refers
to bile. Cholesterol is also a building block of many hormones, signaling molecules
that the body releases to regulate processes at distant sites. Finally, like
phospholipids, cholesterol molecules are found in the cell membrane, where their
hydrophobic and hydrophilic regions help regulate the flow of substances into and
out of the cell.

5. Terpenes
​Terpenes are small hydrophobic molecules found mainly in plants. They include
vitamin A, carotene and plant oils such as geraniol, camphor and menthol.

6. Glycolipids

These are sugar-fat compounds found in the cell membrane.

Introduction

Water is the most common liquid on our planet, vital to all life forms. Firstly, it is a vital
component of living cells. Secondly, it is the dispersion medium for all biochemical
reactions and takes part in many of these reactions. Thirdly, it provides an environment for
organisms to live in. Based on these benefits it is meaningful to explore some of its
chemical and physical properties.

Chemical composition
Water is made up of two hydrogen atoms and one oxygen atom. These are covalently
bonded to give water its chemical formula H​2​O. Water has a slightly positive and negative
charge because the oxygen atom has a greater electronegativity or electron-attracting
power than the hydrogen atoms. As a result, the oxygen atom tends to attract the single
electrons of the hydrogen atoms, so giving the oxygen a slight negative charge while the
hydrogen atoms is left with a slight positive charge. Molecules with charged regions are
called ​polar molecules. water molecule has two separate charged regions (Slightly
positive charged hydrogen atoms and slightly negative charged region of oxygen atom).
These two separate charges makes water a ​dipolar molecule​.

Hydrogen bonds between water molecules

Opposite charges of water molecules are attracted to form hydrogen bonds.

● Opposite charges attract each other. Water molecules are attracted to each other by
the slightly positive charged regions of the hydrogen atoms of one water molecule
and the slight negatively charged region of an oxygen atom of another water
molecule.

● Hydrogen bonds are formed between the water molecules.

 Covalent bonds link the two hydrogen atoms and the oxygen atom to form a
molecule of water. Hydrogen bonds link one water molecule to another water
molecule

● Hydrogen bonds are individually weak. However, when many hydrogen bonds are
formed the resulting union can be sufficiently strong and quite stable.

● The polarity and hydrogen bonds enhance the properties of water to carry out many
biological functions in living things

Water's cohesive and adhesive properties

Have you ever filled a glass of water to the very top and then slowly added a few more
drops? Before it overflows, the water forms a dome-like shape above the rim of the glass.
This water can stay above the glass because of the property of cohesion. In cohesion,
water molecules are attracted to each other (because of hydrogen bonding), keeping the
molecules together at the liquid-gas (water-air) interface, although there is no more room in
the glass. Cohesion allows for the development of surface tension, the capacity of a
substance to withstand being ruptured when placed under tension or stress. This is also
why water forms droplets when placed on a dry surface rather than being flattened out by
gravity. When a small scrap of paper is placed onto the droplet of water, the paper floats on
top of the water droplet even though paper is denser (heavier) than the water. Cohesion
and surface tension keep the hydrogen bonds of water molecules intact and support the
item floating on the top. It's even possible to "float" a needle on top of a glass of water if it is
placed gently without breaking the surface tension .

Surface Tension –The weight of the needle is pulling the surface downward; at the same
time, the surface tension is pulling it up, suspending it on the surface of the water and
keeping it from sinking. Notice the indentation in the water around the needle.

Water has a High Surface Tension and Cohesion

● Surface tension is a measure of how difficult it is to stretch or break a liquid surface.

The high surface tension is due to water molecules forming hydrogen bonds with
other water molecules. Water molecules stick together because of high cohesive
forces between the molecules.

● The surface film (skin) formed due to hydrogen bonding of water molecules allows
some aquatic organisms such as pond skaters, mosquitoes and praying mantis to
stay on the surface of water without sinking in order to move and to find food.
These cohesive forces are related to water's property of adhesion, or the attraction between
water molecules and other molecules. This attraction is sometimes stronger than water's
cohesive forces, especially when the water is exposed to charged surfaces such as those
found on the inside of thin glass tubes known as capillary tubes. Adhesion is observed
when water "climbs" up the tube placed in a glass of water: notice that the water appears to
be higher on the sides of the tube than in the middle. This is because the water molecules
are attracted to the charged glass walls of the capillary more than they are to each other
and therefore adhere to it. This type of adhesion is called capillary action.

Adhesion –Capillary action in a glass tube is caused by the adhesive forces exerted by the
internal surface of the glass exceeding the cohesive forces between the water molecules
themselves.
 Adhesion and Cohesion

● Water sticks to other polar molecules, ionic molecules and to surfaces such as the
sides of its containers. This attraction of water molecules to other substances is
called adhesion.
● Water molecules stick to other water molecules; this attraction is called cohesion.
● The properties of adhesion and cohesion allow capillarity so that water from the soil
can move upward in xylem vessels against gravity.

Why are cohesive and adhesive forces important for life? Cohesive and adhesive forces are
important for the transport of water from the roots to the leaves in plants. These forces
create a "pull" on the water column. This pull results from the tendency of water molecules
being evaporated on the surface of the plant to stay connected to water molecules below
them, and so they are pulled along. Plants use this natural phenomenon to help transport
water from their roots to their leaves. Without these properties of water, plants would be
unable to receive the water and the dissolved minerals they require. In another example,
insects such as the water strider use the surface tension of water to stay afloat on the
surface layer of water and even mate there.

Cohesion & Adhesion – Water's cohesive and adhesive properties allow this water strider
(Gerris sp.) to stay afloat.

Water's solvent properties

Water is a Solvent

Water being a dipolar molecule allows it to be an excellent solvent. Polar and ionic
substances have electrostatic charges (positive and negative charges) and are attracted to
the charges of water molecules. This allows them to dissolve readily in water.

● Polar substances such as sugars and ionic substance such as sodium chloride
dissolve readily in water so they are hydrophilic substances (water loving).
● When sodium chloride (NaCl) dissolves in water, the ions (Na+ , Cl-) separate and
layers of water molecules surrounds the ions.
● Layers of water molecules with the negative ends will surround the sodium ion (Na+)
while layers of water with positive ends will surround the chloride ion (Cl-). These
layers of water molecules prevent the ions from clumping together and keep the
particles in solution.
● Non-polar substances such as lipids have no charge and will not dissolve in water.
Non-polar substances are called hydrophobic substances (water hating). This is
important in hydrophobic interactions in cell membrane which make it selectively
permeable.
● The majority of chemical reactions in the cell take place in aqueous solution. The
solvent property of water allows it to be the main transport medium in organisms. For
example, plasma of blood which dissolve oxygen, nutrients and hormones. In
addition, water acts as a solvent in the alimentary canal; saliva contains water which
helps to moisten food. Water also acts as a solvent in the excretory system For
example, in the excretory system urea dissolves in blood plasma.
● In plants water is used to dissolve minerals salts in the soil and transport these
mineral salts in xylem vessels. Water also transports manufactured food in the
phloem.

Water, which not only dissolves many compounds but also dissolves more substances than
any other liquid, is considered the universal solvent. A polar molecule with partially-positive
and negative charges, it readily dissolves ions and polar molecules. Water is therefore
referred to as a solvent: a substance capable of dissolving other polar molecules and ionic
compounds. The charges associated with these molecules form hydrogen bonds with water,
surrounding the particle with water molecules. This is referred to as a sphere of hydration,
or a hydration shell, and serves to keep the particles separated or dispersed in the water.

When ionic compounds are added to water, individual ions interact with the polar regions of
the water molecules during the dissociation process, disrupting their ionic bonds.
Dissociation occurs when atoms or groups of atoms break off from molecules and form
ions. Consider table salt (NaCl, or sodium chloride): when NaCl crystals are added to water,
the molecules of NaCl dissociate into Na​+ and Cl –​ ions, and spheres of hydration form
around the ions. The positively-charged sodium ion is surrounded by the partially-negative
charge of the water molecule's oxygen; the negatively-charged chloride ion is surrounded
by the partially-positive charge of the hydrogen in the water molecule.

Dissociation of NaCl in water – When table salt (NaCl) is mixed in water, spheres of
hydration form around the ions.

Since many biomolecules are either polar or charged, water readily dissolves these
hydrophilic compounds. Water is a poor solvent, however, for hydrophobic molecules such
as lipids. Nonpolar molecules experience hydrophobic interactions in water: the water
changes its hydrogen bonding patterns around the hydrophobic molecules to produce a
cage-like structure called a clathrate. This change in the hydrogen-bonding pattern of the
water solvent causes the system's overall entropy to greatly decrease, as the molecules
become more ordered than in liquid water. Thermodynamically, such a large decrease in
entropy is not spontaneous, and the hydrophobic molecule will not dissolve.

Water's polarity
 Nonpolar Molecules – Oil and water do not mix. As this macro image of oil and water
shows, oil does not dissolve in water but forms droplets instead. This is due to it being a
nonpolar compound.

One of water's important properties is that it is composed of polar molecules. The two
hydrogen atoms and one oxygen atom within water molecules (H​2​O) form polar covalent
bonds. While there is no net charge to a water molecule, the polarity of water creates a
slightly positive charge on hydrogen and a slightly negative charge on oxygen, contributing
to water's properties of attraction. Water's charges are generated because oxygen is more
electronegative, or electron loving, than hydrogen. Thus, it is more likely that a shared
electron would be found near the oxygen nucleus than the hydrogen nucleus. Since water is
a nonlinear, or bent, molecule, the difference in electronegativities between the oxygen and
hydrogen atoms generates the partial negative charge near the oxygen and partial positive
charges near both hydrogens.
As a result of water's polarity, each water molecule attracts other water molecules because
of the opposite charges between them, forming hydrogen bonds. Water also attracts, or is
attracted to, other polar molecules and ions, including many biomolecules, such as sugars,
nucleic acids, and some amino acids. A polar substance that interacts readily with or
dissolves in water is referred to as hydrophilic (hydro- = "water"; -philic = "loving"). In
contrast, nonpolar molecules, such as oils and fats, do not interact well with water, as
shown in . These molecules separate from it rather than dissolve in it, as we see in salad
dressings containing oil and vinegar (an acidic water solution). These nonpolar compounds
are called hydrophobic (hydro- = "water"; -phobic = "fearing").

Thermal properties of water

Water has a High Heat Capacity.

 ● Specific heat capacity is the amount of heat required to raise the temperature of 1kg
of water by 1°C. The high specific heat of water means that a large increase in heat
energy results in a relatively small rise in temperature. Most of the heat energy is
used to break hydrogen bonds while a small amount is left over which does not
have a significant impact in increasing the temperature of water.
● The high specific heat of water also tends to stabilize ocean temperatures, creating a
favourable environment for marine life. Thus, because of its high specific heat, the
water that covers most of Earth keeps temperature fluctuations on land and in water
within limits that permit life.
● Water also provides a constant external environment for many cells and organisms.
Biochemical processes therefore operates over a smaller temperature range,
preventing extreme temperature changes which will inhibit metabolic activities. This
prevents sudden changes in body temperature caused by external factors like sun or
wind or internal factors like heat released during vigorous muscle activity

The capability for a molecule to absorb heat energy is called heat capacity, which can be
calculated by the equation shown in the figure . Water's high heat capacity is a property
caused by hydrogen bonding among water molecules. When heat is absorbed, hydrogen
bonds are broken and water molecules can move freely. When the temperature of water
decreases, the hydrogen bonds are formed and release a considerable amount of energy.
Water has the highest specific heat capacity of any liquid. Specific heat is defined as the
amount of heat one gram of a substance must absorb or lose to change its temperature by
one degree Celsius. For water, this amount is one calorie, or 4.184 Joules. As a result, it
takes water a long time to heat and a long time to cool. In fact, the specific heat capacity of
water is about five times more than that of sand. This explains why the land cools faster
than the sea. C=QΔT.

The resistance to sudden temperature changes makes water an excellent habitat, allowing
organisms to survive without experiencing wide temperature fluctuation. Furthermore,
because many organisms are mainly composed of water, the property of high heat capacity
allows highly regulated internal body temperatures. For example, the temperature of your
body does not drastically drop to the same temperature as the outside temperature while
you are skiing or playing in the snow. Due to its high heat capacity, water is used by warm
blooded animals to more evenly disperse heat in their bodies; it acts in a similar manner to
a car's cooling system, transporting heat from warm places to cool places, causing the body
to maintain a more even temperature.
Room temperature

● Water is a liquid at room temperature due to the presence of hydrogen bonds

between water molecules. These hydrogen bonds constantly break and reform and
allow water to remain as a liquid.
● Water is a liquid over a wide range of temperature between 0°C and 100°C; this
range of temperatures provide a liquid environment inside cells and serve as a
habitat for aquatic organisms.
Latent heat of vaporization
● Latent heat of vaporization is a measure of the​ amount of heat energy that is
needed to vaporize a liquid​ so that it becomes a gas. A large amount of heat
energy is needed to break the hydrogen bonds in water in order for it to vaporize.
Energy must be transferred to water molecules to allow the hydrogen bonds to be
broken for water to be vaporized.

● Our bodies generate heat because we are homiothermic (warm-blooded) creatures.

The rate at which heat is produced depends primarily on our metabolic rate. Some
of the energy generated by muscular activity will be directly translated into work and
the excess energy will be dissipated as heat. When the temperature tends to exceed
 the optimal, the body will use latent heat of vaporization to cool the body so that it
can be adjusted to its normal temperature. This happens when we sweat. The water
in sweat absorbs body heat and use this heat energy to break the hydrogen bonds in
the water so that it can change to vapour . As the vapour leaves the body heat is
carried away with it to the environment.

● The high heat of vaporization, the implication being of water, facilitates life by
allowing for efficient heat transfer from an organism to the environment during
overheating. This is the case for sweat in terrestrial animals, which evaporates from
the skin of a warm animal. The high heat of vaporization forces the outermost layers
of the epidermis to lose the equivalent amount of thermal energy, cooling the skin.
In addition, gaping in some reptiles such as crocodiles and panting in some
mammals such as dogs.

● Evaporation of water from the leaves of plants through transpiration removes excess
heat allowing cooling to take place.

● Evaporative cooling moderates temperature in lakes and ponds and prevents

terrestrial organisms from overheating.

● The high latent heat of vaporization of water means that a body can be considerably
cooled with a minimal loss of water.
Latent heat of fusion
The latent heat of fusion is ​a measure of heat energy required to melt a solid​. It require a
large amount of heat energy to thaw ice. Conversely, liquid water must lose large amount of
heat energy to freeze.

Due to the large amount of energy required to change liquid water to ice; contents of cells
and aquatic environments a are therefore less likely to freeze in cold weather. Ice crystal if
develop inside of a cell will allow the cells to be damaged significantly. As a result of this
damage the cell cannot function.

Density and freezing properties

Up to 4 degree Celsius

As water-cools from room temperature to 4 degrees Celsius, it becomes denser, as most

liquids, the molecules have less kinetic energy and are closer together. The positive ends of
some water molecules attract the negative ends of other water molecules and hydrogen
bonds form. When water reaches 4 degrees Celsius, the molecules have been pushed as
closest to one another and water becomes most dense in liquid state.

Below 4 degree Celsius

Below 4 degrees, each H​2​O molecule begins to form more stable hydrogen bonds, with up
to four other molecules. At zero degrees Celsius, the H​2​O molecules are lined up in a rigid
frozen crystal lattice, an open hexagonal (six-sided) structure of ice, which holds the water
molecules further apart than in liquid water. This is why water expands when it freezes. Due
to the open spaces within the hexagonal structure in ice; ice is less dense than liquid water
and will float on water.

Below 4 deg C water forms stable bonds and when frozen forms a rigid lattice with long
bonds and space
 The hydrogen bonds arrange six water molecule to form a hexagonal lattice . The
combination of each six water molecule for crystal lattice called ice.

Expansion on freezing:

● since ice floats, it forms at the surface of ponds and lakes, thus insulating the
organisms in the water below it, and allowing the ice to thaw rapidly when
temperature rises.
● Ice floats, it forms on the surface first And the bottom last. If aquatic habitats froze
from the bottom upward aquatic life could not exist.
● Changes in density also maintain circulation in large bodies of water. As the surface
ice melts the colder water sinks and the water rises. This may also result in the
cycling of nutrients.
● floating ice also means that animals that live on ice have somewhere to stand such
as penguins and polar bears

Ice is less dense than liquid water and floats on top of water during winter season.
Tensile strength

● Due to the presence of numerous hydrogen bonds, water molecule has a strong
bonding which provides it a tensile strength.
● As a result of water high tensile strength continuous columns of water can be pulled
all the way up to the top of a tree in xylem vessels during transpiration without the
water columns breaking or pulling apart.
● Water high tensile strength also allows blood to flow in blood vessels.
● Tensile strength of water molecule can be seen in process of surface tension

Reagent

Water is involved in the chemical reactions of metabolism such as photosynthesis and

hydrolysis reactions such as digestion.
PH

● Pure water has a pH of 7, which is neutral, and has exactly the same number of H+
ions as OH- ions floating around in solution.
● Many biological solutions, such as blood or the cytosol inside of cells, have a fairly
neutral pH – one that is neither strongly acidic nor strongly basic. Many
environments, as well, such as the ocean, lakes and streams, and some soils exhibit
fairly neutral pH levels. Many of the enzymes and other macromolecules that
organisms depend on for life processes are most stable in neutral solutions,
therefore mechanisms to maintain neutral pH levels around these molecules have
evolved in many types of organisms. Of course, there are exceptions. The digestive
enzymes in your stomach, for instance, are most effective at low pH, corresponding
to the acidic conditions in your stomach that contribute to the breakdown of ingested
food.
Colour

Water is ​colourless​ and ​transparent​ which allows light to filter into aquatic environments,
and thus aquatic plants can absorb light and perform photosynthesis.

Viscosity
Viscosity measures the resistance to flow for a liquid. The lower the viscosity the faster a
liquid will flow.. Water molecules can slide easily over each other due to the breakage and
reforming of hydrogen bonds. The low viscosity allows water to be a useful lubricant
biological systems. For example, synovial fluid (lubricates many vertebrate joints), pleural
fluid(minimizes friction between lungs and thoracic cage or the ribs, during breathing),
mucus (permits easy passage of faeces down the colon and lubricates the penis and vagina
during intercourse.

Tests for reducing and non-reducing sugars and starches

Reducing and non-Reducing Sugars

Sugars can be classified as either reducing or non-reducing based on their ability to reduce
copper(II) ions to copper (I) ions during the Benedict's Test.
Reducing sugars​ contain free aldehyde or ketone group and have the ability to reduce
copper(II) ions to copper (I) ions during the Benedict's Test. All monosaccharides are
reducing sugars while only some dissacharides are reducing sugar.

Examples of reducing sugar are:

1. Monosaccharides

● Glucose
● Fructose
● Galactose

2. Dissacharides

● Lactose
● maltose

Non-reducing sugars​ do not contain have free aldehyde groups and upon testing with
Benedict’s solution will not reduce copper(11) ions to copper (1) ions.

Non-reducing sugars do not react with any of the reducing-sugar test solutions. However, a
non-reducing sugar can be using dilute hydrochloric acid. After hydrolysis and
neutralization of the acid, the product may be a reducing sugar that gives normal reactions
with the test solutions (Benedict’s solution /Fehling solution).

● Sucrose is the most common disaccharide non-reducing sugar.

Test for reducing sugar

Procedure

1. A liquid food sample does not need prior preparation except dilution if viscous or
concentrated. For a solid sample prepare a test solution by crushing the food and
adding a moderate amount of distilled water. Decant the suspension to remove large
particles. Use the decanted liquid as the test solution.
2. Add 2 cm3 of the sample solution to a test tube.
3. Add an equal volume of Benedict's solution to the test tube and swirl or vortex the
mixture.
4. Leave the test tube in a boiling water bath for about 5 minutes, or until the colour of
the mixture does not change.
5. Observe the colour changes during that time as well as the final colour.
6. To prepare a control, repeat steps 3-5 using 2 cm3 of distilled water instead of
sample solution
Observation:

The initial blue coloration of the mixture turns green, then yellowish and may finally form a
brick red precipitate.

Basis of test:

Benedicts solution contains copper sulphate. Reducing sugars reduce soluble blue copper
sulphate containing copper (II) ions (Cu2+) to insoluble red - brown copper oxide
containing copper (I). The latter is seen as a precipitate.

Test for Starch

Test for Starch:

Iodine/potassium iodide test.

1. Add 2cm​3​ of 1%starch solution to a test tube.

2. Add a few drops of iodine/potassium iodide solution. Alternatively add the latter to
the solid for of starch.

Observation:

A blue-black colouration.

Basis of test:

A polyiodide complex is formed with starch.

Test for a lipid:

Emulsion test:

1. Add 2cm​3​ fat or oil to a test tube containing 2cm​3​ of absolute ethanol.
2. Dissolve the lipid by shaking vigorously.
3. Add an equal amount of cold water.

Observation:

A cloudy white suspension.

Basis of test:
Lipids are immiscible with water. Adding water to a solution of the lipid in alcohol results in
emulsion of tiny droplets in the water which reflect light and give a white , opalescent
appearance.

Test for a protein

Biuret test:

1. Add 2cm​3​ protein solution to a test tube.

2. Add an equal volume of 5% potassium hydroxide solution and mix.
3. Add 2 drops of 1% copper sulphate solution and mix. No heating is required.

Observation:

A mauve or purple colour develops slowly.

Basis of test:

A test for peptide bonds. In the presence of dilute copper sulphate in alkaline solution,
nitrogen atoms in the peptide chain forms a purple complex with copper(II) ions (Cu2+).
Buiret is a compound derived from urea which also contains the –COHN- group and gives
positive results. If protein is not presence you will not see a mauve colour.

Summary
Testing for Using what Method Results
Protein Biurets reagent Add biurets reagent A purple colour
to the solution indicates protein is
present
Lipids Ethanol - the Add ethanol to the If a cloudy and white
emulsion test solution, and shake, solution occurs
then add water between the ethanol
and water, lipids are
present
Starch Iodine solution Add the iodine A blue black colour is
solution to the quickly produced if it
substance suspected comes into contact
of containing starch with starch
Reducing sugar Benedict's reagent Add benedict's If reducing sugars
reagent to the are present, the
solution you are substance will turn to
brick red.
 testing and heat it in
a water bath.
Non-reducing sugar Benedict's reagent Heat the sugar If reducing sugars
solution with dilute are present, the
hydrochloric acid, substance will turn to
then add sodium brick red
hydroxide to
neutralise it, and then
perform the test for
reducing sugars.

Triglyceride

A ​triglyceride​ is one of the most common dietary lipid groups and the type found most
abundantly in body tissues. This compound, which is commonly referred to as a fat, is
formed from the synthesis of two types of molecules.

● A glycerol backbone at the core of triglycerides, consists of three carbon atoms.

● Three fatty acids, long chains of hydrocarbons with a carboxyl group and a methyl
group at opposite ends, extend from each of the carbons of the glycerol.

Triglycerides. Triglycerides are composed of glycerol attached to three fatty acids via
dehydration synthesis. Notice that glycerol gives up a hydrogen atom, and the carboxyl
groups on the fatty acids each give up a hydroxyl group.

Triglycerides form via dehydration synthesis. Glycerol gives up hydrogen atoms from its
hydroxyl groups at each bond, and the carboxyl group on each fatty acid chain gives up a
hydroxyl group. A total of three water molecules are thereby released.

Fatty acid chains that have no double carbon bonds anywhere along their length and
therefore contain the maximum number of hydrogen atoms are called saturated fatty acids.
These straight, rigid chains pack tightly together and are solid or semi-solid at room
temperature. Butter and lard are examples, as is the fat found on a steak or in your own
body. In contrast, fatty acids with one double carbon bond are kinked at that bond. These
monounsaturated fatty acids are therefore unable to pack together tightly, and are liquid at
room temperature. Polyunsaturated fatty acids contain two or more double carbon bonds,
and are also liquid at room temperature. Plant oils such as olive oil typically contain both
mono- and polyunsaturated fatty acids.

Fatty Acid Shapes. The level of saturation of a fatty acid affects its shape. (a) Saturated
fatty acid chains are straight. (b) Unsaturated fatty acid chains are kinked.

Whereas a diet high in saturated fatty acids increases the risk of heart disease, a diet high
in unsaturated fatty acids is thought to reduce the risk. This is especially true for the
omega-3 unsaturated fatty acids found in cold-water fish such as salmon. These fatty acids
have their first double carbon bond at the third hydrocarbon from the methyl group (referred
to as the omega end of the molecule).

Finally, ​trans​ fatty acids found in some processed foods, including some stick and tub
margarines, are thought to be even more harmful to the heart and blood vessels than
saturated fatty acids. ​Trans​fats are created from unsaturated fatty acids (such as corn oil)
when chemically treated to produce partially hydrogenated fats.

As a group, triglycerides are a major fuel source for the body. When you are resting or
asleep, a majority of the energy used to keep you alive is derived from triglycerides stored
in your fat (adipose) tissues. Triglycerides also fuel long, slow physical activity such as
gardening or hiking, and contribute a modest percentage of energy for vigorous physical
activity. Dietary fat also assists the absorption and transport of the nonpolar fat-soluble
vitamins A, D, E, and K. Additionally, stored body fat protects and cushions the body’s
bones and internal organs, and acts as insulation to retain body heat.
Fatty acids are also components of glycolipids, which are sugar-fat compounds found in the
cell membrane. Lipoproteins are compounds in which the hydrophobic triglycerides are
packaged in protein envelopes for transport in body fluids.

What are Proteins?

What are Proteins?

● Protein are made up of the elements : C, H, O, N, S

● Proteins consist of one or more polypeptide chains : they are polymers made up
of amino acid monomers
● There are 20 different types of amino acids
● Amino acids can be classified into four general groups based on the properties of the
"R" group in each amino acid. Amino acids can be polar, nonpolar, positively
charged, or negatively charged. Polar amino acids have "R" groups that are
hydrophilic, meaning that they seek contact with aqueous solutions. Nonpolar amino
acids are the opposite (hydrophobic) in that they avoid contact with liquid. These
interactions play a major role in protein folding and give proteins their 3-D structure.
General structure of amino acid

Proteins are polymers made up of nitrogen-containing monomers called amino acids. An

amino acid is a molecule composed of an amino group and a carboxyl group, together with
a variable side chain. Just 20 different amino acids contribute to nearly all of the thousands
of different proteins important in human structure and function. Body proteins contain a
unique combination of a few dozen to a few hundred of these 20 amino acid monomers. All
20 of these amino acids share a similar structure. All consist of a central carbon atom to
which the following are bonded:
 Amino acid structure

● H:​ Hydrogen attached to the central carbon

● COOH:​ carboxyl group
● NH2:​ amide or amino group
● A variable R:​ group ( side chain)

For each amino acid below the R group or side chain is written in red.

The amino acid alanine .

The amino acid cysteine

The amino acid glycine

Peptide bonds

Dipeptides
 ●
When two amino acids combine a dipeptide is formed.
● The bondings of the amino acids take place by dehydration synthesis/condensation
reaction in which a molecule of water is removed.
● The bond that is formed between the two amino acids is called peptide bond or
amide linkage.

Polypeptides

Many amino acids join together to form polypeptides. Polypeptides are also formed by
dehydration synthesis/condensation polymerization reaction in which molecules of water are
removed resulting in a peptide bond.

● Formation of a Peptide Bond

● In condensation polymerization reaction/ dehydration synthesis, the hydrogen from
the amino end of one amino acid combines with the hydroxyl group of the carboxylic
group end of another amino acid
 Fig 2: The formation of a dipeptide by condensation reaction, resulting in a peptide bond.

Breakage of a Peptide Bond

The polypeptide chain can be broken down into their individual amino acids by the process
of hydrolysis in which water is added to the polypeptide chain.

The structure and function of glucose

All carbohydrates contain carbon, hydrogen and oxygen. Carbohydrates include, sugars,
starch, glycogen and cellulose.

Types of Carbohydrates

● Monosaccharides
● Disaccharides
● Polysaccharides
 Monosaccharides

The term carbohydrate means “hydrated carbon.” Recall that the root hydro- indicates
water. A carbohydrate is a molecule composed of carbon, hydrogen, and oxygen; in most
carbohydrates, hydrogen and oxygen are found in the same two-to-one relative proportions
they have in water. In fact, the chemical formula for a “generic” molecule of carbohydrate is
(CH2O)n. Carbohydrates are referred to as saccharides, a word meaning “sugars.” Three
forms are important in the body. Monosaccharides are the monomers of carbohydrates.
Disaccharides (di- = “two”) are made up of two monomers. Polysaccharides are the
polymers, and can consist of hundreds to thousands of monomers.

Monosaccharides

A monosaccharide is a monomer of carbohydrates. Five monosaccharides are important in

the body. Three of these are the hexose sugars, so called because they each contain six
atoms of carbon. These are glucose, fructose and galactose (shown below). The remaining
monosaccharides are the two pentose sugars, each of which contains five atoms of carbon.
They are ribose and deoxyribose.
 Five Important Monosaccharides

Disaccharides

A disaccharide is a pair of monosaccharides. Disaccharides are formed via dehydration

synthesis and the bond linking them is referred to as a glycosidic bond (glyco- = “sugar”).
Three disaccharides are important to humans. These are sucrose, commonly referred to as
table sugar; lactose, or milk sugar; and maltose, or malt sugar. As you can tell from their
common names, you consume these in your diet; however, your body cannot use them
directly. Instead, in the digestive tract, they are split into their component monosaccharides
via hydrolysis.
Polysaccharides

Polysaccharides can contain a few to a thousand or more monosaccharides. Three are

important to the body:

● Starches are polymers of glucose. They occur in long chains called amylose or
branched chains called amylopectin, both of which are stored in plant-based foods
and are relatively easy to digest.
● Glycogen is also a polymer of glucose, but it is stored in the tissues of animals,
especially in the muscles and liver. It is not considered a dietary carbohydrate
because very little glycogen remains in animal tissues after slaughter; however, the
human body stores excess glucose as glycogen, again, in the muscles and liver.
● Cellulose, a polysaccharide that is the primary component of the cell wall of green
plants, is the component of plant food referred to as “fiber”. In humans,
cellulose/fiber is not digestible; however, dietary fiber has many health benefits. It
helps you feel full so you eat less, it promotes a healthy digestive tract, and a diet
high in fiber is thought to reduce the risk of heart disease and possibly some forms of
cancer.
 Three important polysaccharides are starches, glycogen and fiber.

What are Polysaccharides?

Polysaccharides can contain a few to a thousand or more monosaccharides. Three are

important to the body:

1. Starch
2. Glycogen
3. Cellulose

Three Important Polysaccharides. Three important polysaccharides are starches, glycogen,

and fiber.
Starch

Starches are polymers of glucose. They occur in long chains called amylose or branched
chains called amylopectin, both of which are stored in plant-based foods and are relatively
easy to digest. Starch is made of two polymers of α-glucose: amylose and amylopectin

Amylose

● A chain of glucose molecules joined by α-1,4-glycosidic bonds which, by hydrogen

bonding, form a helix. It is this helix which holds and forms a complex with iodine
when we test for starch.
● The unbranched structure of amylose causes the polymer to exist as a long, coiled
helix under conditions when it can be stabilized. One substance that will stabilize an
amylose helix is iodine, which fits into the hollow core of the structure. Binding of
iodine to amylose helices produces an intense blue color and has long been used as
a qualitative test for starch.

Structure/Function

Insoluble in water, therefore good storage compound. The amylose helix forms a compact
shape which allows tight packing and is therefore an excellent storage molecule.
 Fig 1 structure of amylase

Fig 2: Amylose helix formed from hydrogen bonding.

Amylopectin

● Made up of alpha glucose

● Amylopectin – glucose molecules joined by α-1,4-glycosidic bonds but after every 25
glucose molecules adjacent chains are connected by α-1,6-glycosidicbonds that is
amylopectin is branched.

Structure/Function

● Amylopectin has many protruding ends (glucose molecules) which can be

hydrolysed rapidly –allows rapid release of glucose to provide energy through
respiration. The exposed free ends of the branched molecule provide a large surface
area for enzymes to hydrolysed quickly releasing energy.
 Fig 3 : Structure of amylopectin

Glycogen

Glycogen is also a polymer of glucose, but it is stored in the tissues of animals, especially in
the muscles and liver. It is not considered a dietary carbohydrate because very little
glycogen remains in animal tissues after slaughter; however, the human body stores excess
glucose as glycogen, again, in the muscles and liver.

What is Glycogen?

● Glycogen is the main storage polysaccharide of animal and fungal cells.

● Glycogen is similar in structure to amylopectin. It is poly (1-4) glucose with 9% (1-6)
branches.
 ● Similar structure to amylopectin (in that it is a polymer of α -glucose) of starch but
has many more branches and the branches are shorter. Glycogen is even more
compact than amylopectin

Structure Function

● Compact storage molecule in mammalian liver and in fungal cells and can be broken
down to release glucose. The structure of glycogen allows faster hydrolysis than
starch which is important as animals may need emergency glucose faster than
plants .
● Because it is so highly branched, it can be mobilised (broken down to glucose for
energy) very quickly because there is an increased surface area from the exposed
ends of the branches for enzymes to act.
 Fig 4 : Structure of Glycogen

Cellulose

Cellulose is a polysaccharide that is the primary component of the cell wall of green plants,
is the component of plant food referred to as “fiber”. In humans, cellulose/fiber is not
digestible; however, dietary fiber has many health benefits. It helps you feel full so you eat
less, it promotes a healthy digestive tract, and a diet high in fiber is thought to reduce the
risk of heart disease and possibly some forms of cancer.

Structure/Function

● The numerous cross bridges formed by hydrogen bonds stabilize the structure of
cellulose and give to rigidity and high tensile strength.
● Hydrogen bonding prevents water entering the molecule. Cellulose is therefore
resistant to enzyme hydrolysis which makes it an excellent structural polysaccharide.
Cellulose cell walls provides protection to all plant cells. Humans cannot digest
cellulose but herbivores have bacteria and protoctists in their digestive system which
produce cellulase (β -1,4-glycosidase). The long unbranched fibrous structure
provides great mechanical strength

Fig 5 : Structure of cellulose with adjacent glucose molecules rotated at 180 degrees.
This allows hydrogen bonds to be formed between the hydroxyl (OH-) groups on adjacent
parallel chains which help to give cellulose its structural stability.
 Fig 6 : Structure of cellulose with numerous hydrogen bonds

DNA replication

The nucleus is the largest and most prominent of a cell’s organelles. The nucleus is
generally considered the control center of the cell because it stores all of the genetic
instructions for manufacturing proteins. Interestingly, some cells in the body, such as
muscle cells, contain more than one nucleus, which is known as multinucleated. Other cells,
such as mammalian red blood cells (RBCs), do not contain nuclei at all. RBCs eject their
nuclei as they mature, making space for the large numbers of hemoglobin molecules that
carry oxygen throughout the body. Without nuclei, the life span of RBCs is short, and so the
body must produce new ones constantly.
The nucleus is the control center of the cell. The nucleus of living cells contains the genetic
material that determines the entire structure and function of that cell.
Multinucleate Muscle Cell. Unlike cardiac muscle cells and smooth muscle cells, which have
a single nucleus, a skeletal muscle cell contains many nuclei, and is referred to as
?multinucleated.? These muscle cells are long and fibrous (often referred to as muscle
fibers). During development, many smaller cells fuse to form a mature muscle fiber. The
nuclei of the fused cells are conserved in the mature cell, thus imparting a multinucleate
characteristic to mature muscle cells. LM ? 104.3. (Micrograph provided by the Regents of
University of Michigan Medical School ? 2012)

Organization of the nucleus and Its DNA

Like most other cellular organelles, the nucleus is surrounded by a membrane called the
nuclear envelope​. This membranous covering consists of two adjacent lipid bilayers with a
thin fluid space in between them. Spanning these two bilayers are nuclear pores. A ​nuclear
pore is a tiny passageway for the passage of proteins, RNA, and solutes between the
nucleus and the cytoplasm. Proteins called pore complexes lining the nuclear pores
regulate the passage of materials into and out of the nucleus.

Inside the nuclear envelope is a gel-like nucleoplasm with solutes that include the building
blocks of nucleic acids. There also can be a dark-staining mass often visible under a simple
light microscope, called a ​nucleolus (plural = nucleoli). The nucleolus is a region of the
nucleus that is responsible for manufacturing the RNA necessary for construction of
ribosomes. Once synthesized, newly made ribosomal subunits exit the cell’s nucleus
through the nuclear pores.

The genetic instructions that are used to build and maintain an organism are arranged in an
orderly manner in strands of DNA. Within the nucleus are threads of ​chromatin composed
of DNA and associated proteins. Along the chromatin threads, the DNA is wrapped around
a set of ​histone proteins. A ​nucleosome is a single, wrapped DNA-histone complex.
Multiple nucleosomes along the entire molecule of DNA appear like a beaded necklace, in
which the string is the DNA and the beads are the associated histones. When a cell is in the
process of division, the chromatin condenses into chromosomes, so that the DNA can be
safely transported to the “daughter cells.” The ​chromosome is composed of DNA and
proteins; it is the condensed form of chromatin. It is estimated that humans have almost
22,000 genes distributed on 46 chromosomes.
 Strands of DNA are wrapped around supporting histones. These proteins are increasingly
bundled and condensed into chromatin, which is packed tightly into chromosomes when the
cell is ready to divide.

DNA replication

In order for an organism to grow, develop, and maintain its health, cells must reproduce
themselves by dividing to produce two new daughter cells, each with the full complement of
DNA as found in the original cell. Billions of new cells are produced in an adult human every
day. Only very few cell types in the body do not divide, including nerve cells, skeletal
muscle fibers, and cardiac muscle cells. The division time of different cell types varies.
Epithelial cells of the skin and gastrointestinal lining, for instance, divide very frequently to
replace those that are constantly being rubbed off of the surface by friction.

A DNA molecule is made of two strands that “complement” each other in the sense that the
molecules that compose the strands fit together and bind to each other, creating a
double-stranded molecule that looks much like a long, twisted ladder. Each side rail of the
DNA ladder is composed of alternating sugar and phosphate groups. The two sides of the
ladder are not identical, but are complementary. These two backbones are bonded to each
other across pairs of protruding bases, each bonded pair forming one “rung,” or cross
member. The four DNA bases are adenine (A), thymine (T), cytosine (C), and guanine (G).
Because of their shape and charge, the two bases that compose a pair always bond
together. Adenine always binds with thymine, and cytosine always binds with guanine. The
particular sequence of bases along the DNA molecule determines the genetic code.
Therefore, if the two complementary strands of DNA were pulled apart, you could infer the
order of the bases in one strand from the bases in the other, complementary strand. For
example, if one strand has a region with the sequence AGTGCCT, then the sequence of the
complementary strand would be TCACGGA.
 Molecular Structure of DNA. The DNA double helix is composed of two complementary
strands. The strands are bonded together via their nitrogenous base pairs using hydrogen
bonds.

DNA replication​is the copying of DNA that occurs before cell division can take place. After
a great deal of debate and experimentation, the general method of DNA replication was
deduced in 1958 by two scientists in California, Matthew Meselson and Franklin Stahl. This
method is illustrated in and described below.
DNA Replication. DNA replication faithfully duplicates the entire genome of the cell. During
DNA replication, a number of different enzymes work together to pull apart the two strands
so each strand can be used as a template to synthesize new complementary strands. The
two new daughter DNA molecules each contain one pre-existing strand and one newly
synthesized strand. Thus, DNA replication is said to be "semiconservative."

Stage 1: Initiation. The two complementary strands are separated, much like unzipping a
zipper. Special enzymes, including ​helicase​, untwist and separate the two strands of DNA.

Stage 2: Elongation. Each strand becomes a template along which a new complementary
strand is built. ​DNA polymerase brings in the correct bases to complement the template
strand, synthesizing a new strand base by base. A DNA polymerase is an enzyme that adds
free nucleotides to the end of a chain of DNA, making a new double strand. This growing
strand continues to be built until it has fully complemented the template strand.

Stage 3: Termination. Once the two original strands are bound to their own, finished,
complementary strands, DNA replication is stopped and the two new identical DNA
molecules are complete.

Each new DNA molecule contains one strand from the original molecule and one newly
synthesized strand. The term for this mode of replication is “semiconservative,” because
half of the original DNA molecule is conserved in each new DNA molecule. This process
continues until the cell’s entire ​genome​, the entire complement of an organism’s DNA, is
replicated. As you might imagine, it is very important that DNA replication take place
precisely so that new cells in the body contain the exact same genetic material as their
parent cells. Mistakes made during DNA replication, such as the accidental addition of an
inappropriate nucleotide, have the potential to render a gene dysfunctional or useless.
Fortunately, there are mechanisms in place to minimize such mistakes. A DNA proofreading
process enlists the help of special enzymes that scan the newly synthesized molecule for
mistakes and corrects them. Once the process of DNA replication is complete, the cell is
ready to divide. You will explore the process of cell division later in the chapter.

Introduction

Plants have evolved different reproductive strategies for the continuation of their species.
Some plants reproduce sexually while others reproduce asexually, in contrast to animal
species, which rely almost exclusively on sexual reproduction. Plant sexual reproduction
usually depends on pollinating agents, while asexual reproduction is independent of these
agents. Flowers are often the showiest or most strongly-scented part of plants. With their
bright colors, fragrances, and interesting shapes and sizes, flowers attract insects, birds,
and animals to serve their pollination needs. Other plants pollinate via wind or water; still
others self-pollinate.

Asexual Reproduction

Vegetative reproduction is a type of asexual reproduction. Other terms that apply are
vegetative propagation, clonal growth, or vegetative multiplication. Vegetative growth is
enlargement of the individual plant, while vegetative reproduction is any process that results
in new plant “individuals” without production of seeds or spores. It is both a natural process
in many, many species as well as a process utilized or encouraged by horticulturists and
farmers to obtain quantities of economically-valuable plants. In this respect, it is a form of
cloning that has been carried out by humanity for thousands of years and by plants for
hundreds of millions of years.

Sexual reproduction and the flower

The flower is the reproductive organ of plants classified as angiosperms. All plants have the
means and corresponding structures for reproducing sexually. The basic function of a flower
is to produce seeds through sexual reproduction. Seeds are the next generation, serving as
the primary method in most plants by which individuals of the species are dispersed across
the landscape. Actual dispersal is, in most species, a function of the fruit (a structural part
that typically surrounds the seed).
Plants and sexual reproduction​: Plants that reproduce sexually often achieve fertilization
with the help of pollinators such as (a) bees, (b) birds, and (c) butterflies.

Cross Pollination

In angiosperms, pollination is defined as the placement or transfer of pollen from the anther
to the stigma of the same or a different flower. In gymnosperms, pollination involves pollen
transfer from the male cone to the female cone. Upon transfer, the pollen germinates to
form the pollen tube and the sperm that fertilize the egg.

Self-Pollination and Cross-Pollination

Pollination takes two forms: self-pollination and cross-pollination. Self-pollination occurs

when the pollen from the anther is deposited on the stigma of the same flower or another
flower on the same plant. Cross-pollination is the transfer of pollen from the anther of one
flower to the stigma of another flower on a different individual of the same species.
Self-pollination occurs in flowers where the stamen and carpel mature at the same time and
are positioned so that the pollen can land on the flower’s stigma. This method of pollination
does not require an investment from the plant to provide nectar and pollen as food for
pollinators. These types of pollination have been studied since the time of Gregor Mendel.
Mendel successfully carried out self-pollination and cross-pollination in garden peas while
studying how characteristics were passed on from one generation to the next. Today’s
crops are a result of plant breeding, which employs artificial selection to produce the
present-day cultivars. An example is modern corn, which is a result of thousands of years of
breeding that began with its ancestor, teosinte. The teosinte that the ancient
Mesoamericans originally began cultivating had tiny seeds, vastly different from today’s
relatively giant ears of corn. Interestingly, though these two plants appear to be entirely
different, the genetic difference between them is minuscule.

Genetic Diversity
Living species are designed to ensure survival of their progeny; those that fail become
extinct. Genetic diversity is, therefore, required so that in changing environmental or stress
conditions, some of the progeny can survive. Self-pollination leads to the production of
plants with less genetic diversity since genetic material from the same plant is used to form
gametes and, eventually, the zygote. In contrast, cross-pollination leads to greater genetic
diversity because the male and female gametophytes are derived from different plants.
Because cross-pollination allows for more genetic diversity, plants have developed many
ways to avoid self-pollination. In some species, the pollen and the ovary mature at different
times. These flowers make self-pollination nearly impossible. By the time pollen matures
and has been shed, the stigma of this flower is mature and can only be pollinated by pollen
from another flower. Some flowers have developed physical features that prevent
self-pollination. The primrose employs this technique. Primroses have evolved two flower
types with differences in anther and stigma length: the pin-eyed flower and the thrum-eyed
flower. In the pin-eyed flower, anthers are positioned at the pollen tube’s halfway point, and
in the thrum-eyed flower, the stigma is found at this same location. This allows insects to
easily cross-pollinate while seeking nectar at the pollen tube. This phenomenon is also
known as heterostyly. Many plants, such as cucumbers, have male and female flowers
located on different parts of the plant, thus making self-pollination difficult. In other species,
the male and female flowers are borne on different plants, making them dioecious. All of
these are barriers to self-pollination; therefore, the plants depend on pollinators to transfer
pollen. The majority of pollinators are biotic agents such as insects (bees, flies, and
butterflies), bats, birds, and other animals. Other plant species are pollinated by abiotic
agents, such as wind and water.

Pollination by Insects

Plants have developed adaptations to promote symbiotic relationships with insects that
ensure their pollination.

1. Bees
Bees are perhaps the most important pollinator of many garden plants and most
commercial fruit trees. The most common species of bees are bumblebees and
honeybees. Since bees cannot see the color red, bee-pollinated flowers usually have
shades of blue, yellow, or other colors. Bees collect energy -rich pollen or nectar for
their survival and energy needs. They visit flowers that are open during the day, are
brightly colored, have a strong aroma or scent, and have a tubular shape, typically
with the presence of a nectar guide. A nectar guide includes regions on the flower
petals that are visible only to bees, which help guide bees to the center of the flower,
thus making the pollination process more efficient. The pollen sticks to the bees’
fuzzy hair; when the bee visits another flower, some of the pollen is transferred to the
second flower. Recently, there have been many reports about the declining
population of honeybees. Many flowers will remain unpollinated, failing to bear seeds
 if honeybees disappear. The impact on commercial fruit growers could be
devastating.

2. Flies
Many flies are attracted to flowers that have a decaying smell or an odor of rotting
flesh. These flowers, which produce nectar, usually have dull colors, such as brown
or purple. They are found on the corpse flower or voodoo lily (​Amorphophallus)​ ,
dragon arum (​Dracunculus)​ , and carrion flower ​(Stapleia, Rafflesia)​ . The nectar
provides energy while the pollen provides protein. Wasps are also important insect
pollinators, pollinating many species of figs.

3. Butterflies and Moths

Butterflies, such as the monarch, pollinate many garden flowers and wildflowers,
which are usually found in clusters. These flowers are brightly colored, have a strong
fragrance, are open during the day, and have nectar guides. The pollen is picked up
and carried on the butterfly’s limbs. Moths, on the other hand, pollinate flowers
during the late afternoon and night. The flowers pollinated by moths are pale or white
and are flat, enabling the moths to land. One well-studied example of a
moth-pollinated plant is the yucca plant, which is pollinated by the yucca moth. The
shape of the flower and moth have adapted in a way to allow successful pollination.
The moth deposits pollen on the sticky stigma for fertilization to occur later. The
female moth also deposits eggs into the ovary. As the eggs develop into larvae, they
obtain food from the flower and developing seeds. Thus, both the insect and flower
benefit from each other in this symbiotic relationship. The corn earworm moth and
Gaura​ plant have a similar relationship.

Non-Insect Methods of Pollination

Plants have developed specialized adaptations to take advantage of non-insect forms of

pollination. These methods include pollination by bats, birds, wind, and water.

1. Pollination by Bats
In the tropics and deserts, bats are often the pollinators of nocturnal flowers such as
agave, guava, and morning glory. The flowers are usually large and white or
pale-colored so that they can be distinguished from their dark surroundings at night.
The flowers have a strong, fruity, or musky fragrance and produce large amounts of
nectar. They are naturally-large and wide-mouthed to accommodate the head of the
bat. As the bats seek the nectar, their faces and heads become covered with pollen,
which is then transferred to the next flower.
2. Pollination by Birds
Many species of small birds, such as hummingbirds and sun birds, are pollinators
for plants such as orchids and other wildflowers. Flowers visited by birds are usually
sturdy and are oriented in a way to allow the birds to stay near the flower without
getting their wings entangled in the nearby flowers. The flower typically has a curved,
tubular shape, which allows access for the bird’s beak. Brightly-colored, odorless
flowers that are open during the day are pollinated by birds. As a bird seeks
energy-rich nectar, pollen is deposited on the bird’s head and neck and is then
transferred to the next flower it visits. Botanists determine the range of extinct plants
by collecting and identifying pollen from 200-year-old bird specimens from the same
site.

3. Pollination by Wind
Most species of conifers and many angiosperms, such as grasses, maples, and
oaks, are pollinated by wind. Pine cones are brown and unscented, while the flowers
of wind-pollinated angiosperm species are usually green, small, may have small or
no petals, and produce large amounts of pollen. Unlike the typical insect-pollinated
flowers, flowers adapted to pollination by wind do not produce nectar or scent. In
wind-pollinated species, the microsporangia hang out of the flower, and, as the wind
blows, the lightweight pollen is carried with it. The flowers usually emerge early in the
spring before the leaves so that the leaves do not block the movement of the wind.
The pollen is deposited on the exposed feathery stigma of the flower.

4. Pollination by Water
Some weeds, such as Australian sea grass and pond weeds, are pollinated by
water. The pollen floats on water. When it comes into contact with the flower, it is
deposited inside the flower.

5. Pollination by Deception
Orchids are highly-valued flowers, with many rare varieties. They grow in a range of
specific habitats, mainly in the tropics of Asia, South America, and Central America.
At least 25,000 species of orchids have been identified.

Flowers often attract pollinators with food rewards, in the form of nectar. However,
some species of orchid are an exception to this standard; they have evolved different
ways to attract the desired pollinators. They use a method known as food deception,
in which bright colors and perfumes are offered, but no food. ​Anacamptis morio​,
commonly known as the green-winged orchid, bears bright purple flowers and emits
a strong scent. The bumblebee, its main pollinator, is attracted to the flower because
of the strong scent, which usually indicates food for a bee. In the process, the bee
picks up the pollen to be transported to another flower.
 Other orchids use sexual deception. ​Chiloglottis trapeziformis​ emits a compound
that smells the same as the pheromone emitted by a female wasp to attract male
wasps. The male wasp is attracted to the scent, lands on the orchid flower, and, in
the process, transfers pollen. Some orchids, like the Australian hammer orchid, use
scent as well as visual trickery in yet another sexual deception strategy to attract
wasps. The flower of this orchid mimics the appearance of a female wasp and emits
a pheromone. The male wasp tries to mate with what appears to be a female wasp,
but instead picks up pollen, which it then transfers to the next counterfeit mate.

Human gestation

Human gestation

Twenty-four hours before fertilization, the egg has finished meiosis and become a mature
oocyte. When fertilized (at conception), the egg, now known as a zygote, travels through the
oviduct to the uterus. The developing embryo must implant into the wall of the uterus within
seven days or it will deteriorate and die. The outer layers of the zygote ( blastocyst ) grow
into the endometrium by digesting the endometrial cells. Wound healing of the endometrium
closes up the blastocyst into the tissue. Another layer of the blastocyst, the chorion, begins
releasing a hormone called human chorionic gonadotropin (hCG) which makes its way to
the corpus luteum, keeping it active. This ensures adequate levels of progesterone that will
maintain the endometrium of the uterus for the support of the developing embryo.
Pregnancy tests determine the level of hCG in urine or serum: if the hormone is present, the
test is positive.
Development of the embryo: In humans, fertilization occurs soon after the oocyte leaves the
ovary. Implantation occurs eight or nine days later. The embryo divides several times as it
travels.

First trimester

The gestation period is divided into three equal periods or trimesters. During the first two to
four weeks of the first trimester, nutrition and waste are handled by the endometrial lining
through diffusion. As the trimester progresses, the outer layer of the embryo begins to
merge with the endometrium and the placenta forms. This organ takes over the nutrient and
waste requirements of the embryo and fetus, with the mother’s blood passing nutrients to
the placenta and removing waste from it. Chemicals from the fetus, such as bilirubin, are
processed by the mother’s liver for elimination. Some of the mother’s immunoglobulins will
pass through the placenta, providing passive immunity against some potential infections.
Internal organs and body structures begin to develop during the first trimester. By five
weeks, limb buds, eyes, the heart, and liver have been basically formed. By eight weeks,
the term fetus applies; the body is essentially formed. The individual is about five
centimeters (two inches) in length and many of the organs, such as the lungs and liver, are
not yet functioning. Exposure to any toxins is especially dangerous during the first trimester,
as all of the body’s organs and structures are going through initial development. Anything
that affects that development can have a severe effect on the fetus’ survival.

First trimester​: Fetal development is shown at nine weeks gestation. At this stage, the
body is essentially formed; however many of the organs are not yet functioning.

Second trimester

During the second trimester, the fetus grows to about 30 cm (12 inches). As it becomes
active, the mother usually feels the first movements. All organs and structures continue to
develop. The placenta has taken over the functions of nutrition and waste, along with the
production of estrogen and progesterone from the corpus luteum, which has degenerated.
The placenta will continue functioning up through the delivery of the fetus.

Second trimester: This fetus is just entering the second trimester, when the placenta takes
over more of the functions performed as the baby develops.

Third trimester

During the third trimester, the fetus grows to 3 to 4 kg (6 ½ -8 ½ lbs.) and about 50 cm
(19-20 inches) long. This is the period of the most rapid growth during the pregnancy.
Organ development continues to birth (and some systems, such as the nervous system and
liver, continue to develop after birth). The mother will be at her most uncomfortable during
this trimester. She may urinate frequently due to pressure on the bladder from the fetus.
There may also be intestinal blockage and circulatory problems, especially in her legs. Clots
may form in her legs due to pressure from the fetus on returning veins as they enter the
abdominal cavity.

Fertilization

Fertilization is the process in which gametes (an egg and sperm) fuse to form a zygote. The
egg and sperm are haploid, which means they each contain one set of chromosomes; upon
fertilization, they will combine their genetic material to form a zygote that is diploid, having
two sets of chromosomes. A zygote that has more than two sets of chromosomes will not
be viable; therefore, to ensure that the offspring has only two sets of chromosomes, only
one sperm must fuse with one egg.

In mammals, the egg is protected by a layer of extracellular matrix consisting mainly of

glycoproteins called the zona pellucida. When a sperm binds to the zona pellucida, a series
of biochemical events, called the acrosomal reaction, take place. In placental mammals, the
acrosome contains digestive enzymes that initiate the degradation of the glycoprotein matrix
protecting the egg and allowing the sperm plasma membrane to fuse with the egg plasma
membrane. The fusion of these two membranes creates an opening through which the
sperm nucleus is transferred into the ovum. Fusion between the oocyte plasma membrane
and sperm follows and allows the sperm nucleus, centriole, and flagellum, but not the
mitochondria, to enter the oocyte. The nuclear membranes of the egg and sperm break
down and the two haploid genomes condense to form a diploid genome. This process
ultimately leads to the formation of a diploid cell called a zygote. The zygote divides to form
a blastocyst and, upon entering the uterus, implants in the endometrium, beginning
pregnancy.
Process of fertilization: (a) Fertilization is the process in which sperm and egg fuse to form a
zygote. (b) Acrosomal reactions help the sperm degrade the glycoprotein matrix protecting
the egg and allow the sperm to transfer its nucleus.

To ensure that no more than one sperm fertilizes the egg, once the acrosomal reactions
take place at one location of the egg membrane, the egg releases proteins in other
locations to prevent other sperm from fusing with the egg. If this mechanism fails, multiple
sperm can fuse with the egg, resulting in polyspermy. The resulting embryo is not
genetically viable and dies within a few days.