BIOLOGY UNIT REVIEW  Increased amounts in diabetes mellitus.

I. CARBOHYDRATES
 A carbohydrate is a large biological molecule,
or macromolecule, consisting only of carbon
(C), hydrogen (H), and oxygen (O).

 general molecular formula, C𝑯_𝟐O, thought to

represent “hydrated carbon”.
 come in simple forms such as sugar, and in
complex form such as starches and fiber
 Carbohydrates are a widely diverse group of
compounds that are present in nature.
 chief energy source of all living organism
FUNCTIONS / USES / IMPORTANCE OF
CARBOHYDRATES
 they serve as a form of stored chemical
energy
2. Fructose
 the most important ketose sugar,a hexose,
and is a reducing sugar.
 Sweetest of all sugars. Fruit juices. Honey.
 Hydrolysis of cane sugar and of inulin.
 Can be changed to glucose in the liver and so
used in the body.
 Main source of energy for the spermatozoa
 Hydrolysis of lactose
 Galactose is more commonly found in the
disaccharide, lactose or milk sugar.
 It is found as the monosaccharide in peas.

 They form part of the structures of some

cell and tissues

 Serve as the backbone of other molecule

 Serves as the “Fuel” of our body 3. Galactose

 an aldose,a hexose, and is a reducing
A. Monosaccharides
sugar.
 carbohydrates that cannot be hydrolyzed to
 more commonly found in the disaccharide,
obtain smaller molecules of carbohydrate.
lactose or milk sugar.
 White crystalline solids , very soluble in
 It is found as the monosaccharide in peas.
water, have sweet taste.
 Galactose is part of nerve and brain
 The simplest carbohydrates
biochemicals, so milk is essential to infants.
 contain several functional groups. They
contain the hydroxyl group represented
as –OH. They also contain a carbonyl
group, which is an oxygen double
bonded to a carbon atom. The carbonyl
group may be an aldehyde or a ketone.

1. Glucose
 the most common carbohydrate and classified
as a monosaccharide, an aldose, a hexose,
and is a reducing sugar.
 utilized for energy purposes.
 It is also known as dextrose, because it is
dextrorotatory.
 Glucose units combine and give rise to:
 Glycogen, Starch, Cellulose
 also called blood sugar as it circulates in the
blood at a concentration of 65-110 mg/mL
of blood.
 Normally trace amounts in urine
 Some Important Monosaccharides
 Glucose is the most abundant monosaccharide
found in nature.
 Glucose is also known as dextrose, blood sugar,
and grape sugar.
 Glucose is broken down in cells to produce
energy.
 Diabetics have difficulty getting glucose in their
cells, which is why they must monitor their
blood glucose levels regularly.
B. Disaccharides  In vertebrates it is stored mainly in the liver
- Sugar composed of 2 monosaccahrides as a reserve of glucose for other tissues.
- Found in food and often added as
sweetener
- Connected by glycosidic bond
1. Sucrose (table sugar)

2. Starch
 A polymeric carbohydrate consisting of a large
number of glucose units joined by glycosidic
bonds. This polysaccharide is produced by
most green plants as energy storage.
 Polysaccharide used for medium term storage
in plants
2. Maltose (the malt sugar)
2 types of starch

 Amylose is a polysaccharide made of α-D-

glucose units, bonded to each other through
α(1→4) glycosidic bonds.

 Amylopectin is a water-
soluble polysaccharide and highly
branched polymer of α-glucose units found
in plants.
3. Lactose (the milk sugar)

C. POLYSACCHARIDES
 are complex carbohydrates, composed of 10
to up to several
thousand monosaccharides arranged in
chains. 3. Cellulose
 Poly” means Many
 is an organic compound with the formula
 “Saccharide” means Sugar (C6H10O5)n,
 a polysaccharide consisting of a linear chain of
2 main purpose several hundred to many thousands
1. Store Energy of β(1→4) linked D-glucose units.
2. Structure and Production

1. Glycogen
 The polysaccharide structure represents the
main storage form of glucose in the body.
 Muscle cell glycogen appears to function as an
immediate reserve source of available glucose
for muscle cells.
 Storage of polysaccharides  also known as triglycerides, molecules made
 Glycogen – Stored in the liver and muscles from the combination of one molecule of
glycerol with three fatty acids.
 Starch- Some plants, root tubers, leaves,
seeds and fruits store starch for later use.  serves as a storage system and reserve
 Cellulose – Primary component of plant supply of energy in the body.
cell walls.  fats are broken down to release energy during
periods of low food consumption.
 acts as an insulation material to allow body
II. LIPIDS
heat to be conserved and protect delicate
 one of the four essential biological molecules internal organs from physical damage.
found organisms  fats in the diet can be converted to other lipids
 Almost all are insoluble in water, soluble that serve as the main structural material in
in non-polar solvents the membranes surrounding our cells.
 Mainly: Carbon , Hydrogen and Oxygen
 Have the greatest variation in their basic
structure
 structure of lipids is very non-polar
 have long hydrocarbon chains that determine
the way they act.
 2 parts: “Head” - glycerol
“tail” -fatty acids
 found in fats, oils, hormones, and even
in cell membranes. Composition

- formed from dehydration reactions between

 Functions of Lipids
1. Storage and Source of energy for long-
term use (e.g. triglycerides)
2. Hormonal roles (e.g. steroids such as
oestrogen and testosterone)
3. Insulation – both thermal
(triglycerides) and electrical
(sphingolipids)
4. Protection of internal organs (e.g.
triglycerides and waxes)
5. Structural components of cells (e.g.
phospholipids and cholesterol)
glycerol (an alcohol with three Cs, each with
an –OH group) forming three ester linkages
with three fatty acids (16-18 Cs, with the last
C as part of a –COOH group) and producing
three molecules of water. component fatty
acids (FA) may be either saturated or
unsaturated.
•Saturated FA (e.g., palmitic acid) have the
maximum number of hydrogen atoms bonded to
each carbon (saturated with hydrogen); there are
no double bonds between carbon atoms.

 Biologically Important Types of Lipids •Unsaturated FA (e.g., oleic acid) have at least
 Fats -Made by bonding fatty acids to an one double bond, H atoms are arranged around the
alcohol. double bond in a cis configuration (same side)
-Common energy source resulting in a bend in the structure.
 Phospolipids -Structural component of
cell membranes
-Molecules used to build the
membranes found around and inside
cells.
 Steroids -Act as hormones in plants
and animals, and is a structural
component of animal cell membranes FAT Types
(cholesterol)
1. Saturated fat
 Waxes -Act as a protective layer
- or animal fat, is composed of a glycerol
against water loss in plant leaves and
backbone with three fully saturated fatty
animal skin
acids attached.
1. Fats
 essential macronutrient - Saturated refers to all the carbons in the
 a subgroup of compounds known as lipids that backbone being sp3 hybridised, with two
are found in the body and have the general hydrogen atoms covalently bonded per
property of being hydrophobic. carbon.
 - This class of fats have higher viscosity
and energy content than their unsaturated
cousins. Due to poor solubility issues, this is
the type of fat that is most commonly
associated with heart disease.
2. Unsaturated fat
- or vegetable fat, is composed of a
glycerol backbone with three fatty acid
chains where there is at least one sp2
hybridized carbon.
- This forms a double bond somewhere in
the chain. Monounsaturated fats have one
double bond in the chain, while
polyunsaturated fats have two or more.
- Naturally occurring unsaturated fats, since
they are produced by enzymes, have
specific stereochemistry.
- Natural fats always show the cis
conformation, which has a higher solubility
in water, and is easily broken down by the
metabolic machinery.
a. MONOUNSATURATED FATTY ACID
- contains one double-bonded pair of carbon
atoms in the hydrocarbon chain, which
reduces the number on hydrogen atoms in the
hydrocarbon chain, making it unsaturated.
- often referred to as “good” fats. They make
up the oils and fats found in avocados and
olive oil.
b. POLYUNSATURATED FATTY ACID
- contains two or more doublebonded pairs of
carbon atoms, so its hydrocarbon chain
contains even fewer hydrogen atoms.
- are found in canola oil and other less viscous
plant oils.
c. TRANS FAT
- chemically produced fats. They are generally
considered to be unhealthy, and are found in
mass produced oil found in processed and
fried foods. Trans fats have a controversial
history. They have even been banned for
consumer use in some countries.
Fats - Examples
 Some typical sources of saturated fats
include:
 fatty cuts of beef, pork, and lamb.
 dark chicken meat and poultry skin.
 high fat dairy foods (whole milk, butter,
cheese, sour cream, ice cream)
 tropical oils (coconut oil, palm oil, cocoa
butter)
 lard.
2. Body Fat
Molecular Formula of Body Fats
 Triglyceride - an ester derived from
glycerol and three fatty acids,main
constituents of body fat in humans.
 Functions of Body Fat
1. Serves as an energy storage
2. Construction material for tissues and
organs
3. Carrier substance for vitamins
Too Much Body Fat
 Heart diseases and stroke
 Obesity
 High blood pressure
 Constipation
 Imbalance of nutrients – especially carbs
Too Little Body Fat
 Poor vitamin absorbtion
 Depression
 Increased cancer risk
3.Phospholipids
  Are complex lipids which contains one or
more phosphate groups.
 Amphipathic in nature (Amphipathic in
nature- molecules that has both polar and
non polar parts ; Phosphate grp.-
chemical compound made up of one
phosphorus annd 4 oxygen atoms Can also
found in milk and egg yolk in the form of
lecithin)
 Main component of the cell membrane
Phospholipids consist of a hydrophilic (or
'water loving') head and a hydrophobic (or
'water fearing') tail.
 Functions and Uses of Phospholipids
1. This helps keep the contents of the cell
working properly and separates the
inside of the cell from the surrounding
environment.
2. Phospholipids form a bilayer that
encloses all living matter within a cell.
3. Phospholipids can be broken down in
the cell and used for energy.
4. It can act as emulsifiers. (disperse oil
droplets in water so that the oil and water
do not form separate layers, Prevent fatty
liver)
5. Perform vital functions within the body.
These important cellular barriers support
all cognitive function, cardiovascular
health, nerve health, liver function and
during digestive process; they form
clusters to help move vitamins, nutrients
and fat-containing molecules through
the body.
4.Steroids
- are hormones that occur naturally in the
body.
- is a biologically active organic compound with
four rings arranged in a specific molecular
configuration.
- Steroids have two principal biological
functions: as important components of cell
membranes which alter membrane fluidity; and
as signaling molecules.
 Steroid is classified into two types:
1. Corticosteroids
- are naturally produced by the body, in the
adrenal cortex above the kidney to be precise,
and include steroid hormones that the body
needs for proper functioning.
 Glucocorticoids - are steroid hormones
that play an important role in controlling the
fat, protein and carbohydrate metabolism in
our body
 Mineralocorticoids - are corticosteroids
that play an important role in balancing the
sodium levels in the body. It enables active
absorption of sodium
2. Anabolic Steroids
- are a group of natural and synthetic steroid
hormones that promote muscle growth and
strength.
- It mimics testosterone in the body to enhance
performance by making muscle cells larger
and by allowing the body to recover quickly
from the stress of exercise
 Cholesterol
- It’s role is to maintain the membrane fluidity
- The most abundant and important steroid in
human’s body.
- HO – is the polar portion ………..Amphipathic
molecule.
Steroids - regulate metabolism, immune response,
reproduction and other essential biological
processes.
Mineralocorticoids
- Maintain normal bodily function – by
supporting cellular processes and protecting
against environmental stresses
- Maintain blood volume – aldosterone (a type
of mineralocorticoid) increases fluid retention
- Prevent sodium loss and electrolyte imbalance
(on kidneys, sweat glands, colon and salivary
glands)
Glucocorticoids
- Promote kidney function
- Anti – inflammatory effects
 - Treat variety of allergic and autoimmune
condition (such as poison ivy, asthma, arthritis
and transplant rejection) by depressing
immune function on the molecular, cellular
and tissue levels
- Regulate metabolism- this process requires a
supply of amino acids, w/c are generated from
the breakdown of muscle and lymphoid tissue
stimulate glucose synthesis in the live
supports lung development during last stages
of pregnancy
- when the fetus must prepare to breathe
oxygen for the first time
- In general, these effects help to limit injury
damage
Androgens
Testosterone
Androsteron e  HARM DONE OR DISEASES AQUIRED
e
- controls male reproductive development
- the testes are the main site of androgen
production stimulates growth and
development on the testes
- Vertebrae and long bones, w/c fuels the
growth spurts
- The larynx and vocal chords, w/c lowers the
voice
- Glands in the skin, w/c causes acne and hair
on face, chest, etc.
- Controls sex drive in both men and women
Additional: it causes decreased hair growth on the
scalp, resulting in receding hairline and baldness
Estrogens
Estrone Estrodiol
- prepare a woman to conceive, carry and raise
a child.
- Stimulates development on women during
puberty growth hormone secretion
- Female reproductive organ
- Breast development
- Fat deposition on hips and thighs
- Changes in bone structure(widening hips,
increases bone density)
- prepare for embryo implantation & causes
physiological changes that promote sperm
motility
- promotes growth of the lining of the uterus
- It increases blood flow to supply the fetus
with nutrients supports heart health
- acting directly on heart muscle and by altering
fats found in the blood.
Progestogens
Progesterone
- prepares and maintains the body for
successful pregnancy by stimulating uterine
development and breast growth supports the
mother's immune system
- to prevent rejection of the child inhibits
uterine contraction until the fetus is ready for
birth
TOO LITTLE AMOUNT OR ABSENCE IN THE
BODY
 Kidney failure, cardiac arrhythmias and
circulatory collapse
collapse - sodium loss and electrolyte imbalance
(on kidneys, sweat glands, colon and salivary
glands)
 Inappropriate blood volume
–steroids increases fluid retention
 Low blood sugar
= by increasing insulin resistance in muscle and
adipose tissue, w/c reduces glucose uptake
 Heart illness
TOO MUCH AMOUNT IN THE BODY
 Growth inhibition
 Weight Gain
 Behavioral Changes
 Diabetes
 Liver and Heart Damage
 Sexual and Reproductive Disorders
 (men) decreased sex drive, diminished
sperm count, breast and prostate
enlargement, decreased hormone levels or
sterility
 (women) irregular menstrual cycles or
infertility, develop masculine qualities, such
 as facial hair or a permanently deepened
voice
 Prevent lactation, which leads to postpartum
depression
III. Proteins
- Proteins are large, complex molecules that
play many critical roles in the body.
- They do most of the work in cells and are
required for the structure, function, and
regulation of the body’s tissues and organs.
- 20 different types of amino acids that can be
combined to make a protein.
- Protein, a word derived from the
Greek proteios, meaning “holding first
place.”
- All living things depend on proteins for their
existence. Proteins are the major molecules
from which living things are constructed.
Elements present
o Proteins are composed of molecules called
amino acids, and each amino acid contains
four elements: hydrogen, oxygen,
nitrogen and carbon. Some might also
contain a fifth element, sulfur.
o Proteins, carbohydrates and fats are made
from three basic elements: carbon,
hydrogen and oxygen. However, all proteins
contain an element not found in
carbohydrates and fats -- nitrogen -- and
some proteins also contain sulfur.
DESCRIPTION AS COMPOUND
 Proteins, among the most complex of all
organic compounds, are composed of amino
acids which contain carbon, hydrogen,
oxygen, and nitrogen atoms.
Amino acids
-Amino acids are the monomers that make up
proteins. Specifically, a protein is made up of one
or more linear chains of amino acids, each of which
is called a polypeptide.
Peptide bonds
 Each protein in your cells consists of one or
more polypeptide chains. Each of these
polypeptide chains is made up of amino
acids, linked together in a specific order.
 The amino acids of a polypeptide are
attached to their neighbors by covalent
bonds known as a peptide bonds.
DEHYDRATION SYNTHESIS - During protein
synthesis, the carboxyl group of the amino acid at
the end of the growing polypeptide chain reacts
with the amino group of an incoming amino acid,
releasing a molecule of water. The resulting bond
between amino acids is a peptide bond.
 FUNCTIONS/USES OF PROTEINS
1. Repair and Maintenance
2. Energy
3. Hormones
4. Enzymes- proteins that increase the rate of
chemical reactions in the body
5. Transportation and Storage of Molecules-
Hemoglobin, Ferritin
6. Antibodies
IMPORTANCE
 Proteins are the essence of life processes.
 They are the fundamental constituents of all
protoplasm and are involved in the structure
of the living cell and in its function.
 Enzymes are made up of proteins.
 Many of the hormones are proteins.
 The cement substances and the reticulum
which bind or hold the cells as tissues or
organs are made up partly of proteins.
 They execute their activities in the transport
of oxygen and carbon dioxide by
hemoglobin and special enzymes in the red
blood cells.
 They are involved in blood clotting through
thrombin, fibrinogen and other protein
factors.
  They act as the defense against infections
by means of protein antibodies.
 They perform hereditary transmission by
nucleoproteins of the cell nucleus.
2. Alanine (Ala)
- α- aminoproprionic acid
- second smallest amino acid

EXAMPLE OF PROTEIN FUNCTION/USES 3. Valine ( Val)

 Amylase, lipase, pepsin – Break down - α- amino- β- methylbutyric acid

nutrients in food into small pieces that can -
be readily absorbed. (Digestive enzyme)
4. Leucine (Leu)
 Hemoglobin – Carry substances
throughout the body in blood or lymph. - α- amino- γ methylvaleric acid
(Transport) 𝑯 𝟐

 Actin, tubulin, keratin – Build different 5. Isoleucine ( Ile)

structures, like the cytoskeleton (Structure)
- α- amino- β- methylvaleric acid
 Insulin, glucagon – Coordinate the
- 𝑯
activity of different body systems (Hormone 𝟐

signaling) 6. Methionine (Met)

 Antibodies – Protect the body from foreign - α- amino- methylthiol butyric acid; one of
pathogens (Defense) the two sulphur containing amino acids
 Myosin – Carry out muscle contraction - 𝑯 𝟐
(Contraction)
7. Phenylalanine (phe)
 Legume storage proteins – Provide food
for the early development of the embryo or - β phenylpropionic acid
the seedling (Storage)
- 𝑯 𝟐

Amino Acids
8. Tryptophan (Trp)
- BUILDING BLOCK of proteins
- α- amino- β-indolepropionic acid
- group of organic molecules that human cells
use to make their own kinds of proteins. - has largest side chain
- In the form of proteins, amino acids comprise
the second- largest component of human 9. Proline (Pro)
muscles, cells and other tissues.
- Pyrrolidine
GENERAL FORMULA
- an imino acid
-
- 𝑯 𝟐
where: 𝑯𝟐 - amino group; C- alpha- carbon;
10. Serine ( Ser)
COOH- carboxyl group; R group- side group and
a hydrogen. - α- amino- β- hydropropionic acid
- - 𝑯

11. Threonine (Thr)

1. Glycine (Gly) - α- amino- β- hydrobutyric acid
- α- aminoacetic acid
- 𝑯
- smallest amino acid
12. Cysteine (Cys)
- 𝑯𝟐 𝑯(𝑯) 𝑯
- α- amino- β- thiopropionic acid
 - 𝑯 𝟐  of the proteinogenic amino acids, 9 are
essential, 11 which are nonessential, and 3
13. Tyrosine (Tyr) of which are not found in the human body.
- α- amino- β- P- hydroyphenyl propionic  although over 100 amino acids exist in
acid nature, the human body requires 20 amino
- 𝑯 acids, called standard amino acids, for
normal functioning.
14. Asparagine (Asn)
 approximately half of these standard amino
- 2, 4- diamino- 4 oxobutanoic acid acids are considered essential amino
acids that cannot be synthesized and must
- 𝑯 𝟐 be obtained from food.

Essential Amino Acids

15. Glutamine (Gln)  Histidine, isoleucine, leucine, lysine,
- 2,5- diamino- 5- oxopentanoic acid methionine, phenylalanine, threonine,
tryptophan, and valine.
- 𝑯 𝟐
Non Essential Amino Acids
16. Aspartic Acid
 Alanine, arginine, asparagine, aspartic acid,
- α- aminosiccinic acid cysteine, glutamic acid, glutamine, glycine,
proline, serine, and tyrosine.
- 𝑯
- are organic compounds containing amine (-
17. Glutamic Acid NH2) and carboxyl (-COOH)
- α- aminoglutaric acid functional groups, along with a side chain
(R group) specific to each amino acid.
- has a carboxylic acid group in its side chain - can be split into two main groups Non-polar
and polar amino acids.
18. Lysine

- α,ϵ- diaminocaproic acid  Non-Polar Amino Acids

- can be also be thought of as
- 𝑯 𝟐 𝟐 “hydrophobic”(H20 haters)
- subgroups :
19. Arginine (Arg)
Alkyl glycine, alanine, methionine,
- α- amino- δ -guanidylvaleric acid isoleucine, valine, leucine, proline.
Aromatic- phenylalanine, tryptophan
- 𝑯 𝟐
 Polar Amino Acid
20. Histidine
o considered as “hydrophilic”(water loving)
- α- amino- β- 4 imidazolylpropionic acid o subgroups:
Neutral- serine, threonine,
- 𝑯 𝟐 asparagine, glutamin cysteine, tyrosine
Acidic- aspartic acid, glutamic acid
Basic- histidine, lysine, arginine

 The amino group of the other amino acid

AMINO ACIDS loses a hydrogen. The nitrogen then
substitutes in place of the hydroxyl group,
 there are also three amino acids
forming a peptide bond. This is why peptide
(selenocysteine, pyrrolysine, and N-
bonds are also known as substituted amide
formylmethionine) which are not found in
linkages. The two amino acids are now
humans, but are non-standard protein-
known as residues as they have lost several
building amino acids found in plants and
atoms and they are now covalently bonded
other organisms.
to each other.
 Polypeptide Bond
- Polypeptides are chains of amino
acids. Proteins are made up of one or more
polypeptide molecules.
The schematic below shows the N-terminal at the
upper left and the C-terminal at the lower right.
The sequence of amino acids in a polypeptide is
dictated by the codons in the messenger RNA
(mRNA) molecules from which the polypeptide
was translated. The sequence of codons in the
mRNA was, in turn, dictated by the sequence of
codons in the DNA from which the mRNA
was transcribed.
Levels of Protein
1. Primary structure
2. Secondary structure
3. Tertiary structure
4. Quaternary structure
IV. MOTIFS & DOMAINS
Motif- motif is a simple combination of few
secondary structural elements with a specific
geometrical arrangement.
- also known as the super secondary
structure in a protein
- held in place by weak interactions
- examples are:
Helix-Turn-Helix Motif
Greek Key Motif
Beta-Alpha-Beta Motif
A. Helix-Turn-Helix Motif
- also called α-α type
- composed of two segments of alpha helix
connected by a turn which is made up of
amino acids
- commonly found in cell proliferation and
establishment of DNA structure
B. Greek Key Motif
- consists of antiparallel beta strands
- forms easily during the protein folding
process
- commonly found in proteins such as
Prealbumin and Nitrite reductase
C. Beta-Alpha-Beta Motif
- - composed of two parallel beta strands
connected by an alpha helix with two turns
- - commonly found in proteins which have a
parallel β-sheet.
Domain- is a structural entity, usually meaning
a part of the protein structure which folds and
functions independently.
- combines several secondary structures and
motifs
examples are:
Armadillo Repeat Domain
Basic Leucine Zipper Domain
Phosphotyrosine-binding Domain
A. Armadillo Repeat Domain
- A domain in a solenoid structure
repetitive amino acid sequence of about
40 residues in length that is found in many
proteins.
- commonly found in
β-catenin
B. Basic Leucine Zipper Domain
- is found in many DNA binding eukaryotic
proteins.
- leucine zipper is created by the
dimerization of two alpha helix monomers
bound to DNA
C. Phosphotyrosine- binding Domain
- is a protein domain that binds
to phosphotyrosine.
- combination of various beta sheets and two
alpha helices commonly found in a multi-
domain called Tensin
SIMILARITIES BETWEEN
MOTIFS AND DOMAINS
 both are parts of polypeptide chains in
proteins
 both are collections of secondary structures
of alpha helices and beta pleated sheets
 both do a self-contained job as a part of
the main polypeptide chain
 if a motif is cleaved (cut) off the
polypeptide chain, it loses its function
 if a domain is cleaved off the polypeptide
chain, it will still be able to do its function

REASONS FOR DIFFERENCES BETWEEN
MOTIFS AND DOMAINS
 the structures of motifs are held by weak
interactions such as hydrogen bonds with
the rest of the polypeptide chain. If the
motif is cut off, the weak interactions are
interrupted, hence, losing specific structure.
Since structure determines function, if the
motif lost its structure it will lose its function
and will no longer be able to perform its
self-contained job.
 on the other hand, the structures of
domains do not depend on the interactions
it has with the rest of the polypeptide chain.
If it is cleaved off, it will still retain its
structure, thus function.
 Mutation - is the permanent
alteration of the nucleotide sequence of
a genome of an organism, virus, or
extrachromosomal DNA or other genetic
elements.
4. Huntington disease is caused by HTT
mutation that involves a DNA segment
known as a CAG trinucleotide repeat. This
segment is made up of a series of three
DNA building blocks (cytosine, adenine, and
guanine).
 Sickle cell anemia, Cystic Fibrosis, and
Tay-Sachs disease are all inherited in an
autosomal recessive manner. Meaning, to
acquire this disease, a person must have a
mutation in both copies of the responsible gene
in each cell.
 Meanwhile, Huntington Disease is
inherited in an autosomal dominant pattern,
which means to one copy of the altered gene in
each cell is sufficient to cause the disorder
Other common diseases which
have developed from mutations:
 Marfan Syndrome
 Hemochromatosis
 Phenylketonuria
 Color-blindness

DISEASES DEVELOPED FROM

MUTATIONS

1. Sickle-cell anemia is a blood condition

which involves a single amino acid
substitution from a glutamic acid to a valine.

SYMPTOMS: Fatigue, headache, abdominal

pain, leg ulcer, numbness

2. Cystic Fibrosis is a common genetic

condition which involves the deletion of just
three DNA bases (a codon) from the Cystic
Fibroris Transmembrane Conductance
Regulator (CFTR) gene.

SYMPTOMS: Persistent coughing, wheezing or

shortness of breath

3. Tay-Sachs disease is a rare inherited

disorder caused by mutations in the HEXA
gene. HEXA gene plays a critical role in the
Central Nervous System. This is a frameshift
mutation. Frameshift mutation is a genetic
mutation of a number of nucleotides in a
DNA sequence that is not divisible by three.

SYMPTOMS: Paralysis, seizure, delayed mental

and social development