1

Some Important Concepts of Biology for AIPMT

HUMAN HEART

It is 1012 cm in size, and is present in the Mediastinum (space) of the thoracic-cavity .

It weighs ~250 g in males and 225 g in females.

The apex of the heart is ~9 cm to the left of the mid line

The heart is covered by a transparent serous membrane, the pericardium (the parietal
mesoderm/peritoneum). The pericardial fluid between heart and the pericardium keeps
the heart moist and protects it from friction and mechanical injury.

The wall of the heart has 3- coatings, Epicardium (Outer), Myocardium (Middle) and
Endocardium (Inner). The myocardium contains cardiac muscles.

The atria and ventricles are divided by Coronary Sulcus.

Two Atria are separated by Interatrial septum. In foetus this septum contains Foramen
ovale (opening) and the blood from right atrium (oxygenated blood from Placenta) passes
to the left atrium. At the time of birth when placenta is detached this passage is closed to
form Fossa ovalis. If Foramen ovale is left open after first few weeks of life, it is referred
as a hole in the heart.

The left side of the heart (Lt. A and Lt. V) contains oxygenated (pure) blood and the right
side (Rt. A and Rt. V) has deoxygenated (impure) blood.

Lt. atrium receives oxygenated blood through 2pairs of pulmonary veins (2 per lung).

Rt. atrium receives deoxygenated blood through 1Precaval or Anterior Vena Cava and
1Post caval or posterior Vena cava (Rabbit has 2Precavals).

Lt. and Rt. ventiricles are separated by interventicular septum.

Rt. pulmonary
artery

Lt. pulmonary
artery
Lt. pulmonary
veins

Superior
vena
cava
Tricuspid
valve
Inferior
vena cava
Eustachian
valve
Chordae
Tendinae

Systemic
aorta

Lt atrium

Rt. atrium

Bicuspid valve
Lt. ventricle

Rt. ventricle

Papillary
muscles

Fig. 18.2 : Internal structure of Human heart (simplified)

Lt.ventricle and Rt. ventricle receive oxygenated and deoxygenated blood from respective
atria.
From Lt.ventricle oxygenated blood is supplied to the body organs through systemic aorta.
From Rt. ventricle deoxygenated blood is supplied to lungs through pulmonary aorta
The wall of the Lt.ventricle, which supplies oxygentated blood to all body organs, is
thickest of all the chambers.
Systemic aorta in Amphibians and reptiles is paired. In birds and mammals it is unpaired
(single).In birds it is right and in mammals it is left.

2
Valves
i. Eustachian valve A flap of this valve is present at the opening of the post caval and
prevents the back flow of the blood. The major portion of this valve is vestigial.
ii. Thebasian valve It is present at the opening of coronary sinus which receives
deoxygenated blood from cardiac muscles.
iii. Atrioventricular valves In Lt. side there is Bicuspid (2flaps) valve between Lt. atrium
and Lt. ventricle. This is also known as Mitral valve. In between Rt. atrium and Rt.
ventricle there is a 3flapped Tricuspid valve. The flaps of both Bicuspid and Tricuspid
valve are attached to Papillary muscles through Chordae Tendinae. These prevent
reverting of the valves during contraction of ventricles.

Bicuspid is the only valve in mamalian heart which always remains in contact of the pure
(oxygentated) blood. All other type of valves come in contact of deoxygenated blood.

(The base of the anterior papillary muscles is connected to the interventricular septum by
a special band of cardiac muscles, called Moderator band.)
iv. Semilunar valves These are present at the base of aorta and each has three pockets which
are filled with blood to prevent its back flow to the ventricles.

Conducting System or Nodal Tissue

Like all other vertebrates, in human also, the heart is Myogenic, i.e. the heart beat is
generated by muscles and not nerves
The heart beat is generated through Sino atrial node (SAN) which is also known as Pace
maker. It is a bundle of specialized cardiac muscles. (These muscles like other muscles,
are not contractile but are specialized for conducting impulses like nerve fibres).
In human SA node is embedded in the wall of Rt. atrium. In frogs heart it is present in
the wall of Sinus Venosus.
Atrioventricular node (AVN) is present in interatrial septum, close to Tricuspid valve.
(The AV node is absent in frogs heart).
From AV node arises a bundle of specialized muscle fibres, called Bundle of His or
Atrioventricular bundle. This runs in the anterior part of inter-ventricular septum and
then bifurcates. The branches ramify in the walls of ventricles as Purkinje fibres.

precaval
LA
S.A. Node
Inter nodal
pathway
A.V.Node

Bundle of His
LV

Post caval
RV

Inter ventricular
septum
Purkinje (Purkyne) fibres

Fig. 18.3 : Conducting system in human heart

Heart Beat

The rate of heart beat in a adult human is ~72 per minute.

The single heart beat is called Cardiac cycle and takes 0.8 sec (60 sec / 72 beats ).
Each Cardiac cycle consists of 3parts.
1. Atrial systole (0.1 sec)
2. Ventricular systole (0.3 sec)

3. Diastole (joint) (0.4 sec)

(The heart beat in newly born child is ~100 per min while in foetus it is ~140 per min.)

Chamber
Systole
Diastole
Atrium
0.1 sec
0.7 sec
Ventricle
0.3 sec
0.5 sec
Stroke volume ~70 ml
It is the amount of blood pumped out from each ventricle per beat.
Cardiac output ~5 litre
It is the output of the heart per unit time (70 ml x 72 beats per min.)
Cardiac index ~ 3.2 litre / m2

It is Cardiac output per square meter of the body surface per min.

i.e. (5 lit. / 1.6 m2).
Factors affecting heart beat
Heart beat increases during excitement, eating, exercise, fever and pregnancy.
Heart beat decreases during sleep and shock.
Heart beat is more in males than in females.
Heart beat increases with the increase of altitude (Heart beat altitude).
The heart beat increases with the decrease of animal size (Heart beat 1/size). If elephant,
human and mouse are compared the heart beat will be highest in mouse and lowest in
elephant.
Heart beat 1/BP (except in exercises, in which both blood pressure (BP) and the rate of
heart beat, increase).
Control of Heart beat

(a) Chemical Control
(i) Adrenaline This hormone stimulates heart beat either directly or through
sympathetic nervous system.
(ii) Thyroxine This increases metabolic rate and hence heart beat.

(b) Nervous Control

Medulla oblongata has two regulatory centre

(i) Accelerator centre It functions through sympathetic nervous system (SNS) and
increases heart beat by the secretion of epinephrine or adrenaline.

(ii) Depressor centre It functions through parasympathetic nervous system (PSNS)
by the secretion of acetylcholine. It decreases heart beat.

Heart Sound

In each cardiac cycle, though the heart produces 4sounds but only 1st and 2nd sound can
be heard by Stethoscope. These sounds are described below:
1. 1st Sound
It sounds like LUBB.
It is of longer duration.
It is of lower frequency (low pitch).
It is louder (volume ).
When ? At the beginning of ventricular systole and coincides with the R wave of
ECG.
Why ? Mainly because of closing of Bicuspid and Tricuspid valves.
2. 2nd Sound
It sounds like DUP.
It is of shorter duration.
It is sharper (high frequency).
It is softer (low volume)
When ? At the end of ventricular systole and coincides with the T wave of ECG.
Why ? Because of closing of the semilunar valves of systemic aorta and pulmonary
aorta.

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E.C.G. (E.K.G.)

The instrument which records electrical activity of the heart muscles is called
Electrocardiograph. The sketch obtained on the graph paper is called electrocardiogram (or
electrokardiogram).

The standard symbols used for ECG are PQRST, where P* represents atrial depolarisation;
QRS* complex represents ventricular depolarisation and T* represents ventricular
repolarisation. (P, R & T are deflection waves).
Atrial systole
(0.1 s)
R
Ventricular systole
(0.3 s) Joint Diastole
P

(0.4 s)

ST Interval
(0.32 s)

PR Interval
(0.18 s)
S

QRS
Interval
(0.08 s)

0.4

0.2

0.6

0.8sec

Fig. 18.4 : An Electrocardiogram (ECG)

Intervals in Normal ECG

Interval
PR (or PQ)

Average duration
0.18 sec (180 mili sec)

QRS

0.08 sec (80 ms)

Event
Atrial depolarisation and conduction through
AV node
Ve n t r i c u l a r d e p o l a r i s a t i o n a n d a t r i a l
repolarisation
Ventricular repolarisation

ST
0.32 sec (320 ms)
Abnormality of ECG
1. In rheumatic heart disease (valves damaged) and arteriosclerotic heart desease (due to
formation of plaque or calcification) there is inflammation of atria and AV node, which
results in the lengthening of PR interval.
2. When heart muscles receive insufficient oxygen (lesser blood supply heart ischaemia),
the ST segment is depressed and T wave is flatenned.
3. In acute myocardial infarction the ST segment is elevated and Q & R waves are enlarged.
4. In case of hyperkalemia (K+) T wave is very tall and slender.
* P - wave occurs slightly before the onset of Atrial contraction (systole).
* QRS - waves (complex) begin slightly before the onset of ventricular systole.
* T-wave occurs slightly before the end of ventricular systole.
R

T
Q S
PQ or PR

(1) Lengthening of PR interval

(Rheumatic Fever)

T
S

ST
(2) ST segment depressed
(Heart ischaemia)

P
Q

T
Q

(3) ST segment elevated

(Myocardial infarction)

Fig. 18.5 : Abnormalities in ECG

P
Q S

(4) T wave taller

(Hyperkalemia)

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Heart Disorders
1.

Heart Ischaemia The blood supply to the heart muscles (myocardium) is reduced
(a) Angina pectoris Blood supply to the heart muscles is reduced because of narrowing
of the coronary artery. In such a case there is no problem in routine work but pain
develops during exercise or exertion.

(b) Myocardial infarction In this case the blood supply is totally blocked and the part
of heart tissue becomes dead. The death results mainly from fibrillation.
2. Heart Block In atrioventricular block there is delay between atrial and ventricular
systole. PR > 0.2 sec. In such a case AV node is either not stimulated or stimulation is
delayed. In bundle branch-block QRS > 0.1 sec.

(If atrial impulse suddenly fails to be transmitted to the ventricles, it is called Ventricular
escape or Adams syndrome).
3. Rheumatic Heart Disease It develops due to recurrence of rheumatic fever. The heart
valves are damaged due to formation of antibodies. It is an autoimmune disorder.
4. Persistent ductus arteriosus In foetus pulmonary aorta and systematic aorta are
connected by ductus arteriosus. At birth it degenerates. Rarely it persists and the blood
supply to systemic aorta is reduced which causes congestion in lungs.
5. Fibrillation - A rapid, irregular, abnormal, asynchronous and ineffective contraction
of cardiac muscles is called fibrillation. Atrial fibrillation may occur due to Rheumatic
heart disease and myocardial infarction. The ventricular fibrillation may be produced by
electrocution. If ventricular fibrillation lasts for more than a few minutes, it can be fatal. It
can be stopped by electric shocks or by electronic defibrillators. The latter can be implanted
in the persons of high risks.
Atherosclerosis It is the disorder of arteries (blood vessels) in which cholesterol (plaque)
is deposited.
Arteriosclerosis It is the hardening of arteries due to calcification in old age. The
elasticity of the vessles is reduced. This may also result from atherosclerosis.
Thrombosis It is the clotting of blood inside the blood vessels.

Enzymes
While going through the chapter pay special attention to the following
Definitions
1. Holoenzyme
4. Co-factor

2. Km value

Differences

1. Competitive and non- competitive inhibition

3. Exoenzymes and Endoenzymes

3. Immobilized enzyme

2. Hydrolases and lyases

Terms

1. Feed back inhibition 2. Turn over number
3. Apoenzyme
Buchner, a German bio-chemist, discovered enzymes in yeast, and stated that living nature
of the cells is not essential for the enzymatic activity.
Kuhne coined the term enzyme (means in yeast).
J. Sumner isolated first enzyme (Urease) in pure crystalline form from Jack beans.
Properties of enzymes

Northrop discovered that all enzymes are proteins. However, RNA, can also act as enzyme,
called ribozyme.

Enzymes are oligodynamic, i.e. they are required in small amounts.

They are metabolic regulators.

They act as catalysts in biological reactions and are, therefore, called Biocatalysts.

Velocity

Velocity

They are pH specific, substrate specific and temperature specific. The optimum temperature
for enzymatic action is ~370C. At 00C the enzymes are inactivated while at 600C or above
most of the enzymes are denatured and their enzymatic activity is lost. (The optimum pH
for most of the enzymes is 7; but for Pepsin/Rennin and Alkaline phosphotase (in Kidney)
it is 2 and 10 respectively).
It must be remembered that pH is a log value and a change of 1 on pH scale will cause a
10 fold change in H+, while a change of 2 in pH will produce 100 fold change in H+).
They can not start a chemical reaction but can regulate the velocity of reaction.
They are reusable.
They can not change equilibrium point of a reversible reaction.

0C

37C

50C

Temp.
Fig. 9.11 : Effect of temperature on Enzyme velocity

pH
Effect of pH on Enzyme velocity

Enzymes versus Inorganic Catalysts

(1) Similarities -

Both can not start a chemical reaction.

Both are oligodynamic.

Both are reusable.

Both can not change equilibrium point of the reaction.
(2) Dissimilarities
Enzymes are complex (protein) compounds while the catalysts are simple and inorganic
in nature.

Enzymes are pH, temperature and substrate specific while the catalysts are not so
specific.

The activity of the enzymes can be regulated but catalysts activity can not be regulated.

Important terms
(1) Proenzymes - They are inactive form of the enzymes, eg. Pepsinogen, Trypsinogen
(2) Isoenzymes - Two enzymes with similar structure and catalytic activity but differing
in some of their chemical properties, e.g. LDH (Lactic acid dehydrogenase or lactate
dehydrogenase) and Aldolases

LDH is of two types M type (in muscles), and H type (in heart). The LDH changes
lactic acid into pyruvic acid.
(3) Lysozymes - These are germicidal enzymes present in sebum, tears, milk and saliva etc.
They destroy bacteria by hydrolyzing their cell wall of polysaccharides .
(4) Exo-enzymes and endo-enzymes - The enzymes which work outside the cells (eg. digestive
enzymes) are exo-enzymes while the enzymes working inside the cells (eg. respiratory
enzymes) are called endo-enzymes.
(5) Holoenzymes - These enzymes are conjugated proteins. Their non-protein part is called
Co-factor.

The co-factor can be inorganic or organic in nature. The organic factor, if permanently
attached to the enzymes, is called Prosthetic group and if temporarily attached (only
during reaction), is called Co-enzyme :

Haem is a prosthetic group in catalases and peroxidases. NAD and NADP are coenzymes. FAD is co-enzyme in flavo-proteins or yellow enzymes.

Most of the co-enzymes are derivatives of vitamin B & C.

The protein part of holoenzymes is called Apo-enzyme
(6) Flavo proteins (Yellow enzymes) They are holoenzymes with co-factor of Riboflavin
(vitamin-B2)
(7) Immobilized enzymes - These enzymes are used in industries. They are protected from
the action of proteases by attaching them to a solid support or a jelly, or binding them with
a covalent bond, or incorporating them into artificial cells.

Turn over number The number of substrate molecules which can be catalyzed by a
single molecule of an enzyme in a unit time. A maximum turn over number (36-milion
mol. /minute) is of Carbonic anhydrase.

The turn over number depends upon the number of active sites.
Structure of enzymes
The enzymes are tertiary proteins.

Active site- It is a specific region in the structure of enzyme to which a substrate (reactant)
binds. The Active site has a specific type and number of amino acids. It is a small site and
covers nearly 5% of the total area in most of enzymes. In certain cases metal (co-factor) may
also participate in the formation of such sites.
Theories about enzymatic action
(i) Emil Fishers Lock and key hypothesis According to this theory the active site of
enzyme acts as a lock while substrate acts as a key. Fisher believed that active site is rigid
or non-flexible.
(ii) Koshlands Induced fit theory The active site, according to this theory, is flexible, i.e
a change can be induced by the substrate, in the configuration of the active site.
Enzymatic action

The energy required for a chemical reaction to proceed is called Activation energy.

The enzymes lower the activation energy. (Remember that enzymes cannot start the chemical
reaction)

With the increase in concentration of substrate the enzymatic velocity also increases. At
a certain value all the active site of the enzyme- molecules are saturated and the increase
in substrate concentration does not increase the velocity of the enzymatic reaction.

(The concentration of substrate at which the velocity of enzymatic action reaches half of
its maximum value, is called Km value or Michaelis constant).

Higher is the affinity of an enzyme for a substrate the lower is its Km value,
1

i.e. Km value
affinity

Reaction without enzyme

Vmax

Reaction with enzyme

Vmax

Velocity

B
C

Km
Substrate Cone (m.mol/lit.)
Effect of substrate concentration
on Enzyme velocity

D
Lowering of Activation Energy by enzyme
S - Substrate

P - Product

C = Energy level of Substrate

D = Energy level of Product
C to A = Active energy in the absence of enzyme
C to B = Active energy in the presence of enzyme
A to B = Lowering of activation energy due to enzyme

Fig. 9.12

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Inhibition of enzymatic action
(1) By denaturation
If enzyme is heated to 600C or above the tertiary conformation of the enzyme (active
site) changes and the property of the enzyme is lost.
(2) By competitive inhibition

A chemical, similar in configuration to the substrate, competes for the active site of
the enzyme.
eg. Malonate (Malonic acid) competes with Succinate (Succinic acid) for the active
site of Succinate dehydrogenase. The malonate is here competitive inhibitor for the
synthesis of Fumarate (Fumaric acid) from succinic acid.
Succinate dehydrogenase

Succinic acid Fumaric acid

(Succinate)

(Fumarate)

(The methanol toxicity is similarly averted by ethanol, a competitive inhibitor, for

the enzyme alcohol dehydrogenase).

Sulpha drugs compete with PABA (Para amino benzoic acid) for the active site of
enzyme present in bacteria. Due to the use of Sulphonamide drugs, like Prontosil,
the product- folic acid (a component of vitamin-B complex) is not synthesized by
bacteria and the effect, like an antibiotic, is antibacterial.
(3) By non-competitive inhibition

Here the chemical does not compete with the substrate for active site. It binds with
the enzyme at the site other than active site.

The inhibitor changes the configuration of the active site or the 3-D shape of the
enzyme.
eg. Cyanides stop the functioning of the respiratory enzymes by binding with the Iron
of the prosthetic group. Ions of Heavy metals (like Hg, Ag and Cu) combine with
the disulphide/thiol group and break that to change the 3-D shape of the enzyme, or
denature it.
(4) Allosteric inhibition (Feed back inhibition)

Allosteric enzymes have Allosteric site with the active site. The chemical binds to
this well defined Allosteric site and inhibits the chemical reaction. The inhibitor in
such reactions is one of the product of a long chain of enzymatic reactions and hence
this inhibition is also known as feed back inhibition e.g. Hexokinase.
Binds to Allosteric site
Hexokinase

Glucose + ATP

Glucose 6- Phosphate + ADP

Fig. 9.13

Classification of enzymes (a) On the basis of the substrate

(1)
Proteases (Proteolytic enzymes) They act on proteins/ peptides, eg. Pepsin, trypsin
and polypeptidase
(2)
Carbohydrases (Sucrolytic enzymes) They acton carbohydrates, eg. Amylase,
maltase and sucrase.
(3)
Lipases (Lipolytic enzymes) - These act on lipids or fats, eg. Steapsin.
(b) On the basis of the type of reactions* (1)
Oxido-reductases eg. Oxidase (like Cytochrome oxidase), dehydrogenase (like
Alcohol dehydrogenase)
(2)
Transferases eg. Phosphorylase, transaminase and hexokinase.
(3)
Hydrolases Cause Enzymatic breakdown with the addition of water, eg. Amylase,
urease, lipase.
(4)
Lyases Cause Enzymatic breakdown without the addition of water, eg.
Decarboxylases, Deaminases

9
(5)
Isomerases eg. Aldolases.

(6) Ligases (synthetases) eg. DNA and RNA ligases. (For synthesis of complex molecule
from the simpler ones.)

*Out of about 2,500 different enzymes named so far, the most abundant group is oxidoreductase. The correct order is 1>2 >4 >3 >6 >5.

Enzymes are named according to the classification designed by Enzyme Commission (EC)
of the IUPAC (International Union of pure and applied chemistry). This classification is
based on the type of reaction which they catalyze.
NUCLEIC ACIDS (DNA & RNA)

They are Informational molecules of universal occurrence.

Present in all cells and viruses.
They are polymers of nucleotides and hence Macromolecules. (The structural unit of
nucleic acids is Nucleotide).

Chemical Structure of Nucleic Acid

The nucleic acid on hydrolysis yields 1Pentose Sugar, 2-types of heterocyclic nitrogenous
bases (Purines and Pyrimidines) and phosphoric acid.

Nucleic Acid

Purines

Pyrimidines

DNA

Adenine and Guanine

Cytosine and Thymine

RNA

Adenine and Guanine

Cytosine and Uracil

1N
2

NH2

N7

O
N

N 4 N
9
3
Purine Ring

N
N

NH2

Adenine

Guanine

I. PURINES
NH2

4
3N

O
CH3

6
N
1
Pyrimidine Ring

Cytosine

N
Thymine

N
Uracil

Fig. 9.7 : II. Pyrimidines

Following are the important differences between DNA & RNA
DNA RNA

1. Double stranded

1. Generally single stranded

2. Sugar-Deoxyribose

2. Sugar-Ribose

3. Pyrimidines - Cytosine and Thymine 3. Pyrimidines Cytosine and Uracil

4. Cytosines are equal to Guanines
4. Cytosines are not equal to Guanines

(being single stranded)

5. Base pairs in millions

5. Base pairs usually 100 to 5000

10
5
CH2OH

4
H H
3
OH

1
H OH
2
OH

Ribose (Sugar)

5
CH2OH

4
H H
3

H
1
H OH
2

OH

Deoxyribose (Sugar)

Fig. 9.8 : Sugars in Nucleic Acids

DEOXYRIBONUCLEIC ACID (DNA)

Mainly localised in nucleus.

Small amount of D.N.A. is also present in Mitochondria and Chloroplast.

Nucleosides

i.


ii.

The combination of pentose sugar with nitrogenous bases (Purines or pyrimidines) is called
nucleoside.
Nucleosides of purines Adenine Adenosine
Guanine Guanosine
Neucleosides of pyrimidines
Cytosine Cytidine
Thymine ( in DNA ) Thymidine
Uracil (in RNA) Uridine

Nucleotides

Phosphate ester of a neucleoside is called neucleotide. Each nucleotide consists of

nitrogenous base, pentose sugar and one or more phosphate groups.

i.

Neucleotides of purines -

Adenosine + 1-phosphate group Adenosine Monophosphate (AMP) or Adenylic acid

Adenosine + 2-phosphate groups Adenosine Diphosphate (ADP)

Adenosine + 3-Phosphate groups Adenosine Triphosphate (ATP)

Guanosine + 1-phosphate group Guanosine Monophosphate (GMP) or Guanylic acid

ii.

Nucleotides of Pyrimidines

Cytidine + 1-phosphate group - Cytidine Monophosphate (CMP) or Cytidylia acid

Cytidine + 2-phosphate groups Cytidine Diphosphate (CDP)

Cytidine + 3-phosphate groups Cytidine Triphosphate (CTP)

Thymidine + 1 Phosphate gp. - Thymidine monophosphate or Thymidylic acid

Uridine + 1 phosphate gp. - Uridine monophosphate or Uridylic acid

In case of Deoxyribose sugar (of DNA) the above names are preceded by d - , i.e.

dAMP Deoxy Adenosine Monophosphate

dTDP Deoxy Thymidine Diphosphate

Nucleic acids (DNA & RNA) are polymers of the nucleotides (Nucleoside monophosphate)

The nucleotides are acids and are negatively charged at neutral pH.

The carbons of pentose sugars are primed as 1 , 2 , 3 , to distinguish them from the
carbons of nitrogenous bases.

11
Connecting Concepts

ATP (Adenosine Triphosphate) is also a nucleotide. It contains 1-Adenine base,
1-Ribose sugar and 3-phosphate bonds. It is energy-rich compound, and is also called as
energy currency. Its II and III bonds are energy rich bonds, each releasing 31 kJ energy
per mol.
PO4

III

II

PO4

PO4

Adenine

1
3

Fig. 9.9 : ATP molecule

Nucleotides are joined together by phosphodiester linkage between 5 and 3 carbon atoms
of pentose sugar. The chain of nuclic acid is abbreviated from 5 end to 3 end, in left to right
order.
A
O

3'

4'

1'
2'

C
O

4'

4'

G
3'

2'
1'
O

3'

3'
Sugar
5'
P

5'

2 nm
DNA double helical structure

5'
Sugar
3'
P

4'

4'

3'

5'

5'

5' end
O

3' end
P

3'

1 complete
turn with
10 base pairs
= 3.4 nm

5' 3'

5'

5'

2 Anti-parallel
strands

3'

Nitrogenous
bases

3'
Sugar
5'
5' 3'

Major
groove

5'
Sugar
3'

Sugarphosphate
back bone

5'

5'

4'

Minor
groove

3'

3'

Hydrogen bonds

5'

2 antiparallel strands with nitrogenous bases

Representation in
short-form

Phosphodiester linkage; A Adenine (Purine); T Thymine (Pyrimidine); G Guanine (Purine); C Cytosine (Pyrimidine);
Fig. 9.10

Edwin Chargaff reported that net amount of adenine was equal to thymine (A = T) and
amount of Guanine was equal to cytosine ( G = C ). This means that total number of purines is
equal to the total number of pyrimidines (A + G = T + C ). As the base composition in DNA of
different species varies, the AT/CG ratio also varies from species to species.

AT/CG ratio = 1.52 in human and 0.93 in E .coli.

Double Helical Structure of DNA

To explain base equivalence ( A / T, G / C ) and other properties of DNA, Watson and
Crick (1953), based on X-ray diffraction studies, proposed double helical structure of DNA.
Such structure has 2 right handed helical polynucleotide chains (strands) around a central
axis resembling a spiral staircase. The two strands of helical are anti parallel, means 5 3
Phosphodiaester bonds (Sugar-phosphate groups) are oriented in opposite direction in 2-strands,
i.e., the 5 end of one strand is opposite to the 3 end of the other strand. The bases are held like
steps (rungs) of spiral staircase by hydrogen bonds. The phosphodiaester bonds (with sugar)
form rails or the sides of ladder. These bonds connect 2-nueleotides Between A & T, there are
2 hydrogen bonds (A = T ) and in between C & G there are 3 hydrogen bonds (C G). The
C G base pair has more stability, due to triple bond, as compared to the A = T base pair.

12

The diameter of double helical structure of DNA is 2 nm ( 20 )

Total distance from 1 base pair to another base pair (step or rise)= 0.34 nm (3.4 )
Total base pairs in 1 complete turn (pitch) = 10 (in B-type DNA)
The distance covered in 10- steps or 10 base pairs or 1 complete turn (Pitch) = 3.4 nm
(34 )
On the bases of number of base pairs and right or left handedness of helicals the DNAs
are of more than 12-forms .The main forms or types of DNA are

Types of DNA Type of Helics No. of Base pairs per turn

Properties
A Type
Rt. Handed
11
B Type
Rt. Handed
10
Most stable and most
common form. (Described
by Watson and Crick.)
C Type
Rt. Handed
1
9
C & D types occur under
3
artificial Conditions
D Type
Rt. Handed
8
Lt. Handed
Z Type
12 (6-nucleotides)
Sugar phosphate rail is ZigRepeating unit dinucleotide Zag hence named Z DNA.
Pitch 45, diameter 18.

On heating, the 2-strands of DNA separate from each other (called Melting), and on
cooling they again hybridize (called Annealing). The temperature at which the 2-strands separate
completely is known as its melting temperature (Tm) which is specific for each sequence. If
one sample of DNA has more Tm, this means it has more C G pairs (having stronger bonds,
i.e. 3-hydrogen bonds, difficult to break ).
RIBONUCLEIC ACID (RNA)

It has single helical structure and is mainly of 3-types.
1. m -RNA ( Messenger RNA )
~ 5% of total RNA

Base sequence complementary to one DNA strand

Length varies according to the length of the polynucleotide used.

Generally exists for a short time.

Life span 1-4 minutes (shortest life)

Number of Nucleotides generally more than 1500, so it is the longest RNA.
2. r -RNA ( Ribosomal RNA )
80% of total RNA.

Base sequence similar in all organism.

Synthesized in nucleolar organizing region (NOR) of the DNA.

Life span several days (longest life)

Most stable RNA

The enzyme Ribozyme is also a r-RNA)
3. t -RNA ( Transfer RNA )
15% of total RNA.

Average 80 nucleotides per molecule

Smallest of all RNAs

More than 20 different t-RNA may be present in a given cell.

Easily soluble, so called soluble RNA (s -RNA) also

Transfers amino acid from cytoplasm to the ribosomal machinery.

Acquires Clover leaf structure by folding upon itself.

The unusual bases present in tRNA are Dihydrouracil, Pseudouridine and Hypoxanthine
etc.
(Feulgan, Aceto-carmine and Aceto-orcein are nuclear stains. Feulgan stain (reaction)
is specifically for DNA, as it stains deoxyribose sugar).

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HORMONAL ACTION

Hormonal action affects metabolic changes in the target cells in three different ways

1. By altering permeability of the plasma membrane

2. Through intracellular (IInd or IIIrd) messengers

3. By altering activity of genes.

On the basis of types of receptors used, the hormones fall into three categories.

1. Peptide / protein-hormones and catecholamines

Insulin, glucagon, growth hormone and parathyroid hormones etc. are peptides
while Adrenaline (epinephrine) is a catecholamine.

Such hormones are insoluble in lipids/fats and can not enter through bilipid-plasma
membrane.

The receptors for such hormones are present in plasma membrane.

2. Steroid hormones

The examples of steroid hormones are estrogen, testosterone and corticoids like
aldosterone and cortisol etc.

These are fat soluble and can pass through bilipid layer of cell membrane to reach
the cytoplasm.

The receptors for such hormones are, therefore, present in cytoplasm (i.e.
intracellularily)

3. Thyroid hormones (T3 & T4)

These hormone can also pass through plasma membrane as they are also fat-soluble.

Their receptors are present inside the nucleus.

Fig. 1.1 Functioning of steroid and Amino acid (thyroid) hormones

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A. Steroids and thyroid hormones

They readily pass through plasma membrane into the cytoplasm of target cells.

Inside cytoplasm steroids bind to intracellular receptor proteins in the presence of

Ca++ and form a complex, which enters into the nucleus and binds to regulatory sites
on the chromosomes.

The binding of the complex alters the pattern of gene expression, by initiating or
suppressing the transcription of certain genes to produce specific types of mRNA.

The thyroid hormones directly affect transcription of the genes as their receptors are
present in the nucleus itself.

The action of lipid soluble hormones is slower but long lasting.

Adrenaline
molecule

Disulphide
bond

-subunit

Receptor

Plasma
Membrane
-subunit
(A) Transmembrane or
Cross Membrane receptor

Adenyl cyclase (enzyme)

Mg
G-protein

ATP

++

c AMP
(II-Messenger)

Degraded by Phosphodiesterase
(Enzyme)

Activation of Protein Kinase A

Glycogen

Glycogen phosphorylase

Glucose 1-phosphate
Glucose

Plasma
(cell)
Membrane
Out side the cell
(B) Mechanism of Adrenaline Action

Fig. 1.2 Functioning of Steroids and thyroid hormones

B. Peptide and catecholamines

I.

The receptors for such hormones are Transmembrane-proteins in the plasma

membrane of the target cells. These receptors undergo conformational change when
they bind with the hormone.

This receptor is a tetramer, made up of 2 and 2 glycoprotein subunits, bound to

each other by disulphide bonds.

The -subunits are extra cellular and bind with the hormone, whereas subunits
are present across the membrane. The intracellular portion of subunit has tyrosine
kinase activity.

In case of Adrenaline the binding of hormone triggers the tyrosine kinase activity of
subunits producing auto-phosphorylation.

Due to activity of -subunit the G proteins (-type) are activated.

Each stimulated molecule of G-protein activates the neighboring molecule of enzyme

Adenyl cyclase, suspended in the inner layer of plasma membrane. (see figure)

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Active Adenyl cyclase, in the presence of Mg++ catalyses hydrolysis of ATP

molecules (in cytosol) into Cyclic AMP (cAMP). The cyclic AMP acts as a IImessenger for hormonal action.

Increased number of cAMP molecules in cytoplasm stimulate the molecules of a

special category of metabolic enzymes, i.e. Protein kinases A.

Active molecules of Protein kinases A activate phophorylase kinases which further

modify the activity of other enzymes for required metabolic processes.

An enzyme phosphodiesterase degrades the additional molecule of cAMP to bring

their number to the normal. This stops the effect of the hormone on the target cell.

In case of adrenaline following is the chain of enzymatic reactions :

(i) 1 mol of Adenyl cyclase produces 102 mols. of cAMP (cAMP activates protein
kinase A).

(ii) 1 mol. of protein kinase A activates 102 mols. of phosphorylase kinases.

(iii) 1 mol. of Phosphorylase kinase activates 102 mols. of Glycogen phosphorylases.

(iv) 1 mol. of Glycogen phosphorylase produces 102 mols. of glucose-1- phosphate,
which finally produce glucose.

From 1 mol. of adrenaline hormone the net-production of glucose mols., is
= (102 102 102 102) = 108 mols.
II. In case of insulin the stimulated receptor molecule activates several molecules of G-proteins,
found at the inner surface of the plasma membrane.

These G proteins activate the enzyme (phosphodiesterase) which converts

phosphoetidyl-inositol 4,5-biphosphate (PIP2) into Diacylglycerol (DG) and
Inositol tri-phosphate (IP3). Both act as IInd messengers.

The IP3 is water soluble and enters into cytoplasm. There it stimulates endoplasmic
reticulum for the release of Ca++, the IIIrd messenger, which activates a chain of
reactions.

DG, another II-messenger, is insoluble in water and stays in plasma membrane. Here
it activates Protein Kinases C, which bring out many metabolic changes in the
cytoplasm.

The following compounds may act as IInd, and some even III-messengers, in hormonal
action :

(i) Cyclic Adenosine Monophosphate (cAMP)

(ii) Cyclic Guanosine Monophosphate (cGMP)

(iii) Diacyl glycerol (DAG or DG)

(iv) Inositol triphosphate (ITP or IP3)

(v) Calcium (Ca++)
Heart muscles use 2-types of II-messengers. The cAMP is the II-messenger
for adrenaline and stimulates heart beat. The cGMP is the II-messenger for
acetylcholine and slows down the heart beat.