Introduction To

Biology 20
Ms. Sliwkanich
sliwkanich.weebly.com

Biology (Prefix: Bios = life,

Suffix: ology = the
study of)
Biology is the study of LIFE.
From simple, single celled bacteria
to complex, multi-cellular plants,
animals and fungi.
Biology can study how these
organisms relate to each other and
to the non-living world around
them

Biologists study how life works.

Genetics, physiology, ecology,

evolution, behaviour and anatomy of
organisms fall within the work of
the biologist, as does the study of
populations and communities of
organisms.

Levels of Biological
Organization

Subatomic particles
Atoms
Molecules
organelles
Cells
Tissue
Organ
Organ System
Individual
Population
Ecosystem
Biome
Biosphere

Characteristics of Living
Things

All living things are composed of cells

All living things respond to their
environments

Homeostasis: organisms maintain their

internal environments despite changes in the
external
environment

All organisms acquire and use energy

All living things have a collection of
chemical reactions called metabolism which:

Breakdown food molecules

Build different molecules
5

6.1 Chemistry of
Life

Living organisms only arise from

other living organisms, but living
things are made from non-living
chemicals called macromolecules.
Chemicals from your surroundings
are altered within your cells:
Bonds are rearranged.
Matter is continually cycled

There are over 200,000 different

chemical reactions that occur in the
human body. All of these reactions are
known collectively as Metabolism. 2
types of metabolic reactions:
Catabolic- the breaking down of large
molecules into smaller ones
Anabolic- the formation of complex
molecules from more simple ones.
8

There are 5 broad groups of

Macromolecules that are referred to
as the chemicals of life although
none are capable of life themselves:
Carbohydrates,
Lipids,
Proteins,
Nucleic acids
and Vitamins/Minerals.
9

Nutrients:
Are any substance that have a useful
function when taken into the cells of
the body.
There
are 5 nutrients that are
Macronutrients: are required in large amounts
arranged in 2 Carbohydrates
groups:
Fats and other Lipids
Proteins
Micronutrients: are required in small amounts
Vitamins
Minerals
Water is essential for life but is not considered to be
a nutrient

10

1) Carbohydrates

Carbohydrates are considered to be the

molecules of energy.
They provide a fast source of energy and
should make up the majority of your diet.
Carbohydrates can be found in foods such as
potatoes, rice, bread, corn and fruit. Your body
cannot make its own carbohydrates and
depends on plants.
During photosynthesis plants use sunlight to
convert water and carbon dioxide into
carbohydrates.
11

All carbohydrates contain Carbon,

Hydrogen and Oxygen and almost
always in the same proportions:
1 Carbon : 2 Hydrogen: 1 Oxygen
(1:2:1 ratio eg) glucose C6H12O6)
Hydrog
en
Oxyge
n
Carbo
n
12

Carbohydrates are either single sugar

units or are polymers of many sugar
units:
Polymer: a molecule composed of
three or more repeating subunits.

Carbohydrates can be identified by

the ose ending Eg) fructose,
lactose, cellulose
13

classified according to
the number of sugar
subunits they have in
them.
A) Monosaccharides (mono- one saccharidesugar)

-Common Monosaccharides include: glucose,

galactose and fructose
-Some monosaccharides have the same
chemical formula but different chemical
arrangements. These are called Structural
Isomers.
14

Structural Isomers

These two sugar Isomers have the same

chemical formula, C6H12O6 , but have
different chemical structures. The
sugar on the left in Glucose and the one
on the right is Fructose.
15

Monosaccharides are also known as

reducing sugars because they are
able to reduce copper compounds by
giving copper an electron.
This changes the copper ions colour
from blue to red. This allows us to
test for the presence of reducing
sugars in foods using an agent called
Reducing
Benedicts
solution.
sugar
turns
Benedicts
solution
red

16

B) Disaccharides- (ditwo)

The combination of two

monosaccharides

Eg) Sucrose is formed by attaching a

glucose molecule with a fructose
molecule
All disaccharides are formed in a
chemical reaction called Dehydration
Synthesis
17

In Dehydration
Synthesis, an OH
group from one sugar
is removed and an H
from another sugar is
removed to enable the
two sugars to react.
When the sugars
combine the H and
the OH also combine
to make a water
molecule
Sugar + Sugar Disaccharide +
water
18

Example 1: Dehydration
Synthesis of a
Carbohydrate:

Dehydration synthesis

The opposite is true if we want to

break a polymer of sugars apart. In
order to separate one sugar from
another we must add a water
molecule. This is called Hydrolysis
(Hydro- water lysis- to cut)
Sugar-Sugar + Water Sugar +
Sugar

21

Example 2: Hydrolysis of a
Disaccharide

Hydrolysis of Sucrose

Glucose

Fructose

C) Polysaccharides (polymany)
Polysaccharides are called complex
carbohydrates
They are formed by linking many
monosaccharide subunits together in
long chains.

24

Some examples include:

Starch: A plant polysaccharide that is
composed of 1000-6000 subunits of glucose.
Plants store energy in the form of starch.
Cellulose: Makes up the cell walls of plants
and bacteria. Formed from many thousands
of glucose molecules combined in long,
straight bonds.
Glycogen: Found in Muscle cells and liver
cells. Animals store energy in this
polysaccharide. Resembles plant starch but
only has 16 -24 repeating subunits of glucose.
Glycogen is a branched polysaccharide.
25

Starch

Cellulose
Glycogen
26

The bonds that hold starch and

glycogen together are easily broken by
all vertebrates.
Only a few organisms can breakdown the
bonds which hold together Cellulose.
Animals which relay on cellulose for the
bulk of their energy must have
specialized stomachs and have
developed symbiotic relationships with
some fungi and bacteria. Eg)
ruminants and some termites
27

2) Lipids
Lipids are a diverse group of
macromolecules that have one
important property in common: they
are insoluble in water and thus float
on water.

28

Lipids store more than double the amount

of energy than any other biological
molecule.
Lipids, called phospholipids are used in the
formation of cell membranes.
Lipids at the base of the skin provide
insulation and Lipids cushion internal
organs
Lipids are involved in the synthesis of some
hormones (estrogen)
Lipids are carriers for vitamins A,D,E and K
29

Many Lipids are composed of 2

structural components: Glycerol and
fatty acid molecules.

These molecules are put together in

much the same way that
carbohydrates are, using the process
of Dehydration synthesis.

A) Triglycerides: Lipids that are

formed when 1 Glycerol molecule is
combined with 3 fatty acid
molecules. Triglycerides make up
the bulk of vegetable oils and animal
fats.
1 glycerol + 3 fatty acids 1 Triglyceride + 3
Water molecules

31

Formation of a Lipid

32

Triglyceride
In a triglyceride, the glycerol always
has the same shape but the
composition of the three fatty acids
may differ. The three fatty acids
may be identical or different, short
or long, unsaturated or saturated.

33

i) Saturated Fatty Acid:

(animal fats)
This means that there are no double
bonds between the carbon atoms in the
fatty acids. Each carbon is bound to as
many hydrogen atoms as it can handle.
Saturated fats are solid at room
temperature and because there are
only single bonds this makes them very
stable and very hard to break down.
Eg) Butter, Lard
34

ii) Unsaturated Fatty Acids:

(plant oils)

Has double bonds between some of

its carbon atoms leaving room for
additional hydrogen atoms. These
double bonds allow the fats to be
liquid at room temperatures. Eg)
Sunflower oil, Canola Oil,
margarine*

35

Margarine
Margarine is a vegetable oil which is solid at room
temperature.

Scientists take an unsaturated plant oil and heat it

into a vapour.
They then introduce extra hydrogen molecules which
break apart the double bonds in the unsaturated
vegetable oils converting them into saturated fats.
This makes the oils solid at room temperature.
Adding hydrogen to these unsaturated oils can cause
them to turn into trans fats. Trans fats are very
dangerous and can lead to many health problems.

36

B) Phospholipids
A special class of lipids where a glycerol is
bonded to a phosphate group and 2 fatty acids.
This arrangement gives the molecule a polar
arrangement.
A polar molecule has an electrical charge
associated with it.
The polar end of the molecule is soluble in water
while the non-polar end is insoluble in water.
These special properties make them perfect for
biological membranes.
37

Phospholipids

38

Fats are an important part of your

diet and should make up 30% of
your total food intake. Recall that
fats are very energy rich
macromolecules and too much fat
intake can cause many problems
such as obesity, and heart disease.

39

C) Cholesterol
Cholesterol is a fat-like material in your
blood. It is required to build and maintain
cell membranes and is a main component
in the production of sex hormones
(estrogen and testosterone)
Your body makes its own cholesterol but
when you eat foods that have lots of fat or
cholesterol, you can have too much build
up in your blood.
40

Cholesterol
Cholesterol can build up on the inside
of blood vessels. This is called
arthrosclerosis.
If too much cholesterol builds up, then
the blood cannot flow through your
blood vessels.

41

Atherosclerosis

42

Not all cholesterol in your blood is bad for you. There

are two kinds of blood cholesterol:
HDL(High Density Lipoprotein) Called good
cholesterol. HDL carries bad cholesterol to the
liver to be broken down. Most HDL is made by
your body and is dependent upon genetics.
LDL(Low Density Lipoprotein) Called bad
cholesterol. About 70% of the cholesterol we get
from food is LDL. LDL can stick to the walls of
arteries and essentially clog the arteries preventing
oxygen carrying blood cells from getting to tissue.
This clog is called a plaque. If a plaque occurs in
arteries delivering blood to the heart muscle or the
brain a heart attack or stroke can occur.
43

3) Proteins

Proteins are used to form the structural parts of cells.

They are used to build structures in new cells and
repair damage to old cells.
Cytoplasmic organelles like the mitochondria and
ribosomes are made primarily of protein.
Muscles, bones, tendons, ligaments, nerves, skin,
connective tissue, finger nails and hair is made of
protein.
Enzymes, antibodies and components of blood are all
made of protein. In fact 80% of the bodys structure is
protein.
Proteins are not used as energy molecules, although as
a last resort the body can break down proteins for
energy.
44

Like other macromolecules, proteins

are made up of smaller subunits
called Amino Acids.
Proteins, like lipids and
carbohydrates, contain carbon,
oxygen and hydrogen. Amino Acids
also contain the element Nitrogen.

45

Amino Acids

All Amino acids have the

same general structure.
All amino acids have a
central carbon which is
bonded to a hydrogen and 3
other groups: An Amino
group, a Carboxyl group and
a R group.
The R group is one or more
atoms and it distinguishes
the 20 types of amino acids
from one another. In other
words, each of the twenty
amino acids have a different
R group.
46

There are 20 different amino acids that make up

all of the known proteins.
These 20 amino acids can be put together in
chains varying in length and order.
Proteins can be as short as a couple of amino
acids in length or can be as long as 250,000
amino acids in length. Changing just one amino
acid can change the entire structure and
function of a protein.
The human body can synthesize 12 of the 20
amino acids but must get the other 8 from diet.
These eight amino acids are called essential
amino acids.
47

Amino acids are combined in a

dehydration synthesis reaction.
A covalent bond forms between the
carboxyl group of one amino acid
and the amino group of the adjoining
amino acid. This bond is called a
peptide bond

48

20 different amino acids

49

Polypeptides
Chains of amino acids are called
polypeptides. Because of molecular
interactions within and between
amino acids along a Polypeptide
chain, the polypeptides twist and
coil into complex 3 dimensional
shapes which form a protein.

50

Complex structures of
Protiens

51

Exposing Proteins to excess heat, radiation or a

change in pH may alter the shape and
configuration of the protein. If the protein
uncoils or changes shape it cannot do what it
was intended.
Permanently changing the structure of a protein
is called coagulation. Temporarily changing its
structure is called denaturation.

When you add heat and

fry an egg you have
changed the proteins in
the egg permanently

52

Nucleic Acids
Nucleic acids include DNA
(deoxyribonucleic acid) and RNA
(ribonucleic acid)

53

Nucleic acids direct growth and development.

Nucleic acids determine how a cell functions
and what characteristics it has.
Nucleic acids contain the information needed
to build proteins.
Nucleic acids have no real energy potential
and are not used by the body as an energy
source.

54

Nucleic acids are formed by joining small subunits

called nucleotides. Nucleotides are composed
of a 5 carbon sugar, a phosphate backbone and a
nitrogen containing base which gives the
nucleotide its individual properties.

55

There are 4 different nucleotides

which combine together to make up
all the DNA of all living organisms
on earth.

56

Vitamins and Minerals

Vitamins and minerals are not

macronutrients and have no energy
value.
They are essential in acting as:
components of body structures (bones and
teeth),
in chemical reactions (coenzymes),
in nerve transmissions,
maintaining water balance and carrying
oxygen and carbon dioxide in the blood.

57

If a person lacks vitamins

and minerals in the diet,
many diseases and
deficiencies can develop.

Eg) vitamin C deficiency causes

scurvy, vitamin K deficiency causes
some blood clotting problems Iron
deficiency causes anemia ,
magnesium deficiency may cause
muscle cramping and spasms

58

Vitamin and Mineral

Deficiency

Folic acid
deficiency
during
pregnancy
Goiter:
Iodine
deficiency

Vitamin B
deficiency
causes
Pellagra

Vitamin D
deficiency
causes Rickets

59

Energy within
the cell

60

Metabolic reactions are the chemical

reactions that occur in cells
Example:
H2O2 + catalayse enzyme H2O + O2
( Hydrogen Peroxide (a toxin) is broken
down into
Water + Oxygen Gas)
61

Enzymes and metabolic

Reactions
Molecules in solids, liquids and gases are
in constant motion due to kinetic energy.
In order for chemical reactions to occur,
atoms must come in contact with one
another.
The chances of two specific atoms colliding
with each other is very low and reactions
very rarely occur spontaneously.
62

Enzymes and metabolic

Reactions
If we heat atoms, they move more
quickly and the chances of a reaction
happening are greatly increased.
This is not an option in biological
systems for as we know, heating up
cells to the point where reactions
occur readily can destroy them.
63

Another way to speed up

reactions is too use a
Catalyst
Catalyst: chemicals that speed up
chemical reactions at low
temperatures without altering the
products formed by the reaction.
Catalysts are not used up or
permanently changed during the
reaction.
64

Catalysts
Catalysts work by lowering the activation
energy needed to get a reaction started.
Activation energy is the amount of energy
need in order to start the reaction.
Think about gasoline reacting with oxygen.
In order to get that reaction to occur, we
need to add a small amount of heat (a
match or spark)
65

Enzymes
Enzymes: Cells manufacture specific
proteins that act as catalysts.
Enzymes regulate reactions which
occur in living things. They permit
low temperature reactions to occur
by reducing the activation energy of
the reactions.

66

Substrates are molecules on

which the enzymes work.

Each substrate molecule combines with

a specific enzyme and the substrate
molecules are changed during the
reaction forming a specific product.
The enzyme is not changed during the
reaction.

There are more than 200 000 reactions

that occur in the human body, each
using a specific enzyme to catalyze it.

67

Characteristics of
enzymes

Enzymes are identified by the suffix

ase, which is added to the substrate
that the enzyme attaches too.
Eg) Carbohydrases break down
carbohydrates, liapases break down
lipids and proteases break down
proteins.
Enzymes are specific for the substrate
they work on
Enzyme action is often reversible
68

How Enzymes Work

Enzymes are proteins and have a special
unique shape. This unique shape makes
enzymes substrate specific.
Enzymes have an area called an active site.
This area acts like a dock allowing
specific substrate molecules to join with
the enzyme.
When the substrate joins the enzyme at the
active site, the enzyme and substrate bond
forming the enzyme-substrate complex
69

Enzymes also increase reaction rates

by bringing substrate molecules
together and aligning them in the
correct way

70

Once the enzyme has completed its

job, the products are release, the
enzyme returns to it normal shape
and is free to pick up another
substrate.

71

Sometimes enzymes require special chemical

helpers in order to work properly. These
helpers bind to either the enzyme or the
substrate to help them fit together better.
Coenzymes: Organic (contain carbon)
molecules that are synthesized from
vitamins. They alter the active site of the
enzyme to ensure a correct fit with the
substrate.
Cofactors: Inorganic molecules such as iron,
zinc and potassium that also help enzymes
bind to substrate
72

Factors that effect Enzyme

Reactions
It is estimated that a single enzyme
can catalyze between 100 and 30
million reaction in one minute.
Reaction rates can vary greatly
depending on the environment the
reactions are taking place in.

73

pH
Enzymes function within an optimal pH range.
Most human enzymes function best in the
range of pH between 6 and 8 (neutral). There
are exceptions to the rule:
Pepsin: an enzyme that breaks down proteins
in the stomach. Can only work in a very acidic
(pH of 1-3) environments
Trypsin: an enzyme that further breaks down
peptides in the small intestine. This enzyme is
most effective in a very basic (pH 9)
environment and will not work below a pH of
6.
74

pH and enzyme activity

75

Temperature
As with pH, enzymes in the human body perform best
at an optimum. The optimum temperature for
reactions is about 37 degrees Celsius.

Even though molecules move faster and have more

energy at higher temperatures, high temperatures
change the shape of enzymes (denature them )
and render them inactive.
This is why high fevers for prolonged periods of
time are extremely dangerous.
Temperatures that are too low effect the flexibility
of the active site and prevent substrate molecules
from fitting properly.
76

Effect of Temp. on Enzyme

activity

77

Competitive Inhibition
Inhibitor molecules have shapes that
are very similar to that of the
substrate. The inhibitors compete
with the substrate for the active
sites of the enzymes.

78

As long as the inhibitor is joined at the

active site, the actual substrate
cannot bind and reactions stop.
This is how Carbon Monoxide
poisoning occurs. Carbon monoxide
binds to the active site of the
hemoglobin enzyme. Oxygen cannot
bind because the Carbon Monoxide
is
taking up the active site.
Substr
ate

Competiti
ve
inhibitor

Enzyme
79

Regulation of Enzyme
Activity

Metabolic pathway a series of

chemical reactions (animation)
Feedback Inhibition: As the products
from a series of chemical reactions
begins to accumulate within a cell, the
product interferes with one of the
enzymes in the reaction sequence.
This interference slows the reaction
rate, preventing the accumulation of
final products.
80

Feedback Inhibition:

The final product does not interfere by binding to

the active site, the final product binds to
another site on the enzyme called the regulatory
site.
If the final product binds to the regulatory site
of the enzyme, the active site is changed
preventing more substrate from undergoing a
chemical reaction.

81

Feedback Inhibition

Metabolic pathway

Product D
accumulates and
inhibits enzyme 1 by
binding to its
regulatory site

Without Enzyme 1
making substrate B,
the metabolic
pathway is shut

82

Allosteric activity (Non- competative

inhibition): anytime something binds to
the regulatory site of an enzyme and
changes that enzymes shape. This can
speed up, or slow down enzyme activity
Feedback inhibition is a form of allosteric
activity.

Enzymes can also be activated using

allosteric activity. Here a precursor
(effector) molecule binds to the
regulatory site, activating the enzyme.
83

84

Competitive and non

competitive Inhibition

85