BIOCHEMISTRY FOR 3RD YEAR

BIOLOGY MAJOR STUDENTS

By: Shiferaw A. (Ass’t. professor)

 Course overview
 Course title-Biochemistry
 Course Code: Biol 3071
 Credit hour=3, Or 5ECTS
 Contact hour/wk=3 (2 theoretical classes + 1 practical/
week)
 Evaluation:
 Continuous assessment (50 %)
 Chapter quiz = 15%
 Test= 20%
 Group assignment = 10%
 Attendance and class participation = 5%
 Final/End of semester Exam (50 %) 2
 Course Outline
1.Introduction
♣ Definition and Scope of Biochemistry
♣ The Cell and its organelles
♣ Water and Chemical bonds in biochemistry
♣ pH and biological buffer ring systems
2.Chemistry of Amino acids and Proteins
3.Enzymes
4.Chemistry of Carbohydrates
5.Metabolism of Carbohydrates
6. Chemistry of Lipids
7. Metabolism of lipid 3
 Definition Biochemistry
 Definition :

 The Simplest definition: Biochemistry is “Chemistry of the living cell”

 The science that study about the chemical constituents of living cells and the reactions

and processes they undergo

 It is essential to understand basic functions in the body

Why do we study Biochemistry?

 We study biochemistry to understand:

♣ the chemical processes that take place in living organisms

♣ the chemical logic of living things includes synthesis and degradation of small

organic molecules

♣ How energy is formed during chemical reaction and their transformation

♣ important issues in medicine, health, and nutrition 4

 Scope of Biochemistry

 The term ‘Biochemistry’ was first introduced by the German

Chemist Carl Neuberg in 1903.
 Biochemistry takes into account the studies related to:
 the nature of the chemical constituents of living matter,
their transformations in biological systems and
the energy changes associated with these transformations
 Biochemistry is related to all of the other sciences that study about
living organisms
E.g. molecular biology, molecular genetics, physiology, toxicology,
drug design, nutrition….
 Many newer disciplines have been emerged from biochemistry such
as:
enzymology (study of enzymes),
endocrinology (study of hormones),
clinical biochemistry (study of diseases),
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 Cellular Organization
 All cell similarities:
Use energy (ATP)
Cells structure and function
Biomolecular organization
 The cell has three major components:
1. The cell membrane/plasma membrane = composed of a phospholipids
lipid bilayer in which proteins are embedded; hence the name fluid
mosaic membrane.
 It limits the size of the cell and
 Controls transport of materials in and out of the cell.
 It is partially permeable and highly regulatory.
2. The Cytoplasm = contains the cellular organelles suspended in a jelly like
fluid called the cytosol
3. Nucleus = has nuclear envelop that separates it from the cytoplasm. It
contains the nucleoplasm (DNA, RNA and proteins).
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7
 The cellular organelles

1) Mitochondria

 Mitochondria (Greek: ‘mitos’-thread;

‘chondros’-granule)

 the power generators/ ATP production

 Surrounded by a double membrane

with a series of folds called cristae.

 Contains its own DNA.

 The outer and inner mitochondrial

membranes, that separate the matrix
from the cytosol. 8
 Mitochondria…
 The outer membrane contains pores made of the protein porin and is freely
permeable to most ions and small molecules.
 Where as the inner membrane is a specialized structure that is highly
impermeable to charged substances (H+, Na+, and K+ )

 Transport across inner mitochondrial membrane requires special carrier

proteins.

 Inner mitochondrial membrane is unusually rich in proteins b/c it is the site

of electron transport chain and oxidative phosphorylation.
 It forms convolutions known as cristae that greatly increase its surface area.
 The mitochondrial matrix:
 gel-like solution in the interior of mitochondria 50% protein (most of
them are enzymes).

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2) Endoplasmic reticulum (ER): is a network of membranous
tubules within the cell.
♣ Rough ER – studded (associated) with ribosomes and hence

serves as site of protein synthesis.

♣ Smooth ER - lacks ribosome. It has role in lipid and steroid

hormone synthesis, detoxification, glycogen storage.

3) Ribosomes: are nucleoproteins (made of ribosomal proteins and

nucleic acids). They are just supramolecular structures.

♣ Present either attached on RER or free in the cytosol.

♣ They serve as site of protein synthesis in both cases.

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4) Golgi apparatus – ‘post office’

♣ It consists of a curved stack of flattened vesicles called

cisternae.

♣ involved in modifying, sorting, and distributing proteins

produced in the RER to lysosomes, secretory vesicles or to
the plasma membrane.

5) Lysosomes – suicide bag/sac

 Contain hydrolytic enzymes and are involved in intracellular

digestion.

 Involved in digestion and elimination of unwanted material

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 6) Peroxisomes
 Involved in oxidative reactions using O2 such as in oxidation of

very long chain fatty acids (>or=20 carbons) to shorter chain

fatty acids, conversion of cholesterol to bile acids…

 These reactions produce H2O2, which is toxic hence used or

degraded by catalase

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 7. Cytoskeleton
 It is a flexible fibrous protein support the cell

 composed of three types of fibrous protein components:

♣ Microtubules composed of tubulin - move and position organelles and

vesicles
♣ Thin filaments (actin microfilaments) composed of actin, form
cytoskeleton
♣ Intermediate filaments composed of different fibrous proteins such as α-

keratin
 Roles of the cytoskeleton include:

 maintains structure or shape of the cell surface,

 fixes the position of organelles

 moves compounds within the cell or moves the cell itself 13

14
Prokaryotic Vs Eukaryotic cells

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 INTRODUCTION

1.3. Water and Chemical bonds in Biochemistry

 Water
 Water is the most abundant substance in living systems, making
up ~ 70% of weight of most organisms.
 Biological importance of water in living things
the transport of nutrients in blood, removal of wastes
the site of enzyme catalyzed reactions (chemical rxn)
the transfer of chemical energy occur
Regulation of body temp
Maintain the structure and function of biomolecules
Dissolves ionic and polar molecules, universal solvent
 Two properties of water are especially important biologically:
1) its polar nature
2) the strong cohesive forces (hydrogen bonding capability)
between water molecules.
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 The polar nature
 The water molecule has a polar structure with
two lone pair electrons on the oxygen atom.

 The oxygen nucleus draws electrons away

from the hydrogen nuclei, which leaves the
region around the hydrogen nuclei with a net
positive charge making the molecule polar.

The cohesive forces

 Due to its polar nature water molecules
interact strongly with one another through
hydrogen bonds.
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 The cohesive forces
 In a solid state (in ice) each water
molecule forms four hydrogen bonds
with the surrounding four water
molecules and networks of hydrogen
bonds hold the structure together.

 Whereas in a liquid state each water

molecule forms less number of
hydrogen bonds because some of them
broken down as it changes from solid to
liquid state.
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 unusual (unique) physical properties of water are:
♣ high surface tension (force acting to push together the liquid
molecules)
 allow water to serve as transport medium
♣ high heat of vaporization (amount of heat needed to convert liquid to
gas phase)
 helps to keep body temperature constant
♣ Water Expand upon freezing
 density decrease as it cools down (max density at 4degree
centigrade)
 allow organisms to live at the bottom of fresh water lakes, protected
from freezing and for ease melting
♣ has high solvent power
 Water is a powerful dissolver of ions & polar compounds & similarly powerful
excluder non-polar molecules
♣ high specific heat capacity that makes it serve as a heat buffer
♣ high melting point and boiling point 20
 Chemical Bonds in Biomolecules
 Living organisms are composed of organic molecules referred to
as biomolecules.
 The major ones are:
Proteins,
Carbohydrates,
Lipids and
Nucleic acids (RNA and DNA).
 Molecular interactions among biomolecules is mediated by two
general types of chemical bonds:
i) Covalent bonds and
ii) Non covalent interactions
 Major d/c is the bond energy (a single covalent bond is far much
strong compared to a single non - covalent bond).

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 Covalent bonds are true chemical bonds present in biomolecules
 is formed by the sharing of a pair of electrons between
adjacent atoms.
 Important covalent bonds in biomolecules include:
 Peptide bonds = b/n amino acids in proteins
 Glycosidic bonds = b/n monosacharides in oligo and
polysaccharides and
 Ester bonds in fats
 Phosphodiester bonds b/n nucleotides in DNA and RNA.
 Because of the dynamic nature of chemical processes occurring
in living cells; readily reversible, non-covalent molecular
interactions are crucial.
 Although non - covalent bonds are individually weak,
collectively these bonds have a very significant role in stabilizing
the structures of proteins, nucleic acids, polysaccharides and
supramolecular structures like membrane lipids and ribosomes.
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 Such weak, non-covalent forces are also the key means by which
molecules interact with one another:
hormones - receptors,
antibodies - antigens.
in the replication of DNA,
the folding of proteins into three-dimensional forms,
the specific recognition of substrates by enzymes, and the
detection of molecular signals
 There are four non covalent weak interactions (2dry ) that mediate
the reversible dynamic interaction of biomolecules:
hydrogen bond,
electrostatic interaction (ionic bond or salt bridge),
hydrophobic interaction and
Vander waals interaction.

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i) Electrostatic interactions - are formed by electrostatic attraction
between two oppositely charged ions.
 In living cells, there are a number of ionizable chemical entities
that bear a positive (e.g., amino, R–NH3+) or a negative (e.g.,
carboxylic, R–COO-, -PO4-) charge.
ii) Hydrogen bonds - are formed between an electronegative atom
(usually oxygen or nitrogen) and a hydrogen atom covalently
bonded to another electronegative atom in the same or another
molecule.
 Hence the H atom in a H-bond is partly shared between two
relatively electronegative atoms.
 Therefore H- bond is represented by broken lines

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iii) Van der Waals interactions - are formed b/n any two atoms in
close proximity within a molecule.
 They are formed due to charge asymmetry around an atom due to
asymmetric distribution of electronic charge.
 This charge asymmetry around an atom in turn acts through
electrostatic interactions to induce a complementary charge
asymmetry in the electron distribution around its neighboring
atoms.
iv) Hydrophobic interaction - Based on their interaction with water
biomolecules can be classified as:
Hydrophilic,
Hydrophobic
Amphipathic

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26
 Hydrophilic - dissolve readily in water because they can replace
energetically favorable water-water interactions with even more
favorable water-solute interactions. E.g. polar molecule

 Hydrophobic - poorly soluble/ insoluble in water b /c it

interferes with favorable water-water interactions and decrease
entropy of the system . E.g., non-polar molecule

 Therefore in aqueous solutions, hydrophobic molecules tend to

cluster together to minimize the energetically unfavorable effects
of their presence .

 This interaction of non-polar biomolecules in aqueous

environment is referred to as hydrophobic interaction 27
 An amphipathic compound - contains both polar and non-polar regions.

 The polar or charged, hydrophilic region interact favorably with the

solvent and tends to dissolve, but non-polar, the hydrophobic region has

the opposite tendency, to avoid contact with water (hydrophobic

interaction).

 Hydrophobic interaction is particularly important in biological membranes

by stabilizing its component amphipathic . e.g. phospholipids bilayer.

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 INTRODUCTION

1.4. Biological buffer systems

 Biological buffer systems

Buffers:

 are a solution of weak acid and base that resists a significant change in pH

upon addition of an acid or a base.

 are mixtures of weak acids and their conjugate bases.

Buffers tend to resist changes in pH when small amounts of acids or bases

added.
weak acids and bases are weak electrolytes and dissociate in aqueous

solution very slightly and they exist in a state of equilibrium in the body.

Ex. mixture of CH3COOH (proton donor) and CH3COO- (proton acceptor)

in dissociation of acetic acid.

This property of weak acids and bases play an important role in

maintenance of the physiologic pH by serving as buffers. 30

 The buffering tendency of any weak acid/base conjugate is
determined by its pKa (dissociation constant)
 pKa- is defined as the appropriate pH at which a given acid shows
maximum dissociation
 Weak acids on the other hand, exhibit a 50% dissociation at their
appropriate pH and hence have generally a lower pKa value.
 The relationship between pH, pKa and the molar ratio of the
acid/base conjugate in a solution is determined as follows according
to the Henderson -Hasselbalch equation.

Equilibrium of any weak acid

 Where HA - represents a weak acid

A- “ conjugate base
K1- “ rate constant for dissociation of the acid
K2- represents the rate constant for association of the
conjugate base and H+ 31
 The equilibrium constant, Ka for the weak acid(HA) is defined
by the following equation

Equation1

 The equation can be rearranged to define [ H+] as follows

Equation 2

 The [ H+] is often reported as pH, which is –log [H+].

 In a similar fashion, -log Ka is represented by pKa.
 Equation 2 can be converted to the negative (-log) form by
substituting pH and pKa: pH= pKa + log[ A-] Equation
-3
[HA] 32
 Equation 3- is the familiar henderson-Hasselbalch equation,
which defines the relation ship between pH, pKa and the ratio
of acid and conjugate base concentrations.
pH= pKa+ log [ A-]
[H A]
 The buffering capacity of a buffer system is best when pKa of an
acid is equal to the pH of the medium.
 [A-] = [HA], such that the ratio of [A-]/ HA] is 1 so pH =
pKa
 This occurs when [proton donor] = [proton acceptor].
 Therefore a buffer system with pKa value close to the
physiological pH =7.4 is a good extracellular (blood plasma)
buffer system.
 E.g. acetic acid/acetate conjugate is not a good buffer system in
blood because the pKa of acetic acid 4.75 is far from 7.4.
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 In mammals (including man) the important buffer systems are:
the bicarbonate buffer system,
the phosphate buffer system and
the amino acid and protein buffer systems

1. The bicarbonate buffer system

 It is the major buffer system in blood plasma; consists of
carbonic acid (H2CO3) and its conjugate base bicarbonate ion
(HCO3-).
 The Henderson-Hasselbalch equation for this conjugate be:
pH = pKa + log [HCO3-]/[H2CO3].
 However, ~99 parts of 100 molecules of H2CO3 in aqueous
solution are formed from CO2 dissolved in water.
 The rxn take place in RBCs catalyzed by carbnonic anhydrase.
 Therefore, in the blood, [CO2] is approximately equal to [H2CO343].
 Thus The H-H equation can be rewritten as: pH = pKa + log

[HCO3-]/[CO2].

 From this equation, we can deduce; In body fluids, pH increases

with the increase in [HCO3-] but decreases as [CO2] increases.

 The bicarbonate buffer looks a weak buffer system in the blood

because:

 pKa of H2CO3 , 6.1 is relatively far from 7.4.

 In addition [CO2] & [HCO3-] in the blood are low or limited.

 However, these concentrations are regulated by lung and kidney

respectively making the bicarbonate buffer an important system
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 2. Phosphate buffer system
 It involves the dissociation of phosphoric acid which has three
ionizable hydrogen atoms:
H3PO4 ↔ H+ + H2PO4- pKa = 2.0
H2PO4- ↔ H+ + HPO42- pKa = 6.8
HPO42- ↔ H+ + PO43- pKa = 12.7
 Q. Which one do you think would be the best buffer system in the
blood and why?
The second is an important buffer in our body b/se 6.8 is very
close to 7.4.
 Phosphate buffer is primarily important intracellular particularly
in kidneys and in urine where their concentration is higher.

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2. CHEMISTRY OF AMINO ACIDS
AND PROTEINS

2.1. Amino acids

 Amino Acids
 Amino acids are the simplest building blocks of proteins.

 The word protein comes from the Greek word ‘proteos’ meaning
“primary/ 1st ”

 The most abundant and important class of organic compounds in

our body, constituting more than half of its cellular dry weight

 Although more than 300 different amino acids have been

described in nature, only 20 are commonly found as constituents
of proteins in living things.
These are (20) the only amino acids that are coded for by
DNA; the genetic material in the cell.
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 Structure of amino acids
 Each amino acid has an hydrogen atom,
a carboxyl group, a primary amino
group, and a distinctive side chain or
radical (“R-group”) bonded to the α-
carbon atom.
 Amino acids have carboxyl and amino
groups bonded to the α-carbon atom-
called α-amino acids
 The side chain or R - group
distinguishes each amino acid
chemically
 All amino acids except proline do have
the structure shown in the figure.
 Proline is an amino acid that contain
imino group (-NH) instead of amino
group (NH2) 39
 Proline is the exceptional amino
acids which has a secondary amino
group called imino-group

 In proline its propionyl side chain

forms an amide bond with its
primary amino group.

 Hence proline is known as an

IMINO ACID

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 Naming amino acids
These 20 amino acids are given both three-letter and one-letter
abbreviations. Thus: alanine = Ala = A

41
 Classification of Amino acids

 Based on R groups amino acids are classified as: (five)

Non-polar

Polar uncharged
Aromatic

Positively charged
Negatively charged

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Non-polar (Hydrophobic) amino acids Further sub classified as:

A). Those that contain a non - polar aliphatic (linear hydrocarbon)

side chain. Includes:

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B). Those that contain aromatic (cyclic or benzene ring and
derivative ring) side chain. Includes:

44
 Polar (Hydrophilic) Amino acids Further classified as:

A. Positively charged (basic)

amino acids - contain an extra
amino group in their side
chain.

 NB: For Histidine the one with

double bond is NH+ at
physiological pH when
histidine is incorporated in the
formation of polypeptides.
45
B. Negatively charged (acidic) amino acids - that contain an extra
carboxylic group in their side chain (in addition to the -carboxylic
group).

46
C. Uncharged amino acids -
contain no charged group in their
side chain.

 Includes:

 Serine and Threonine with

OH functional group
 Cysteine with SH functional

group
 Asparagine and Glutamine

with extra amino group.

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 The side chain of cysteine contains
a sulfhydryl group (–SH).

 In proteins, the –SH groups of two

cysteines can become oxidized to
form a dimer, cystine, which
contains a covalent cross-link
called a disulfide bond (–S–S–)
through spontaneous (non-
enzymatic) oxidation of their
sulfhydryl groups

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 Arginine and Histidine are semi-essential. The healthy adult
human body synthesizes just enough arginine and histidine but
in:
the childhood growth period,

sickness,

convalescence (recovery) and

during pregnancy

 such amount is not enough and requires dietary

supplementation and hence these amino acids become
essential. Therefore, these two amino acids are semi-essential.
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 Proteins
 Proteins are polymers of amino acids. They are formed by linkage of
the constituent amino acids by a peptide bond.
 Peptide bond is an amide bond formed by the covalent linkage of (–
OH) α-carboxyl group of one amino acid with the(-H) α-amino
group of another amino acid through condensation reaction (water is
released).
 Requires an input of free energy


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51
 The series of three or more amino acids joined by peptide bonds is
referred to as a polypeptide chain.(more than 50 amino acids)

 If two amino acids are joined together they form a dipeptide

where as if it is three amino acids, tripeptide.

 A polypeptide chain has polarity (has a carboxyl or C- terminal

and a amino or N-terminal ends).

 By convention, the amino end (N-terminal) is considered as the

beginning of a polypeptide chain.

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 Protein structure (orginzation)

 Proteins are polypeptides with specific amino acid sequences.

 Amino acid sequence determines the final three-dimensional

structure of a protein

 Protein structure is generally described as having four levels

Primary

Secondary
Tertiary
Quaternary

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54
 1. Primary Structure
 Is the sequence of amino acids in the polypeptide

 It is formed by α-carboxyl of one amino acid + α -amino group of

another amino acid by the peptide bond.

55
 2. Secondary Structure

 Regular arrangement of amino acids within localized regions

 Polypeptide chains fold Into regular periodic structures such as

 The α helix (alpha helix) and

 The β pleated sheet (beta pleated sheet)

i) Alpha Helix : Is a spiral rod like

structure in which tightly packed
coiled polypeptide backbone with
the side chains extend outward in a
helical array to avoid interfering
sterically with each other
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 ii. Beta Sheets
 Are almost fully extended
structures in which the
backbone of the polypeptide
chain is extended into a
zigzag/pleated form unlike
coiled -helix
 The side chains extended out
ward in opposite directions.
 Also known as β pleated
sheet b/c the surfaces appear
pleated

57
 3. Tertiary structure
 Is formed by folding of secondary structures into a large three-dimensional
organization that is mainly stabilized by non-covalent interactions
 It is the final three dimensional and functional structure of proteins.
 The polypeptide chain folds so that its hydrophobic side chains are buried and
its polar, charged chains are on the surface.

Forces that stabilize protein structure

 In addition to the peptide bond protein structure is stabilized by different types
of covalent and/or non-covalent bonds.
 These are:
Disulfide bond
Hydrogen bond
Electrostatic interaction (Ionic bond or salt bridge) and
Hydrophobic interaction
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59
 4. Quaternary structure
 Occurs in proteins that have multiple polypeptide chains, called
subunits.
 The structure formed by monomer-monomer interaction in an
oligomeric protein is known as quaternary structure
 Proteins with identical subunits are termed homooligomers but
those with d/t or distinct polypeptide chains are termed
heterooligomers

60
 Example: Quaternary structure (hemoglobin)
 Hemoglobin is composed of
four polypeptide chains, each
of which is bound to a heme
-group.
 The two α-chains and the two
β-chains are identical

61
 Denaturation of proteins
 Protein denaturation is the unfolding and disorganization of the
secondary and tertiary structures of proteins due to breaking
down of the non covalent bonds that stabilize them.
There is no hydrolysis of the peptide bonds and hence the
primary structure is preserved.
 Denaturing agents include:
Heat,
Organic solvents,
Mechanical mixing,
Strong acids or bases,
Detergents, and
Ions of heavy metals such as lead and mercury.
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Denaturation could be reversible, however most proteins, once
denatured, remain permanently disordered.

Hence denaturation is usually irreversible.

A cooked egg cannot be “uncooked”.
Denatured proteins are often insoluble and therefore precipitate from
solution. 63
 Classification of proteins
 Proteins can be classified based on different criteria such as:

over all morphology (shape and size ).

function,

chemical composition,
biological or nutritional value.

A. Based on overall shape and size (Axial Ratio):

 Based on their overall structure or shape proteins are generally classified as:

 Globular proteins and

Fibrous proteins.

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 Globular proteins
 Spherical in shape and resemble
irregular balls with <10 axial ratio.
 More liable to denaturation and
are easily soluble in water.
 water.
Most of the globular proteins
serve as enzymes, hormones,
transporters etc.
 Examples are immunoglobulins,
albumin, hemoglobin and
insulin.
 Shape usually is composed of
different secondary structures.
Fibrous proteins
 Have linear and elongated
structure with >10 axial ratio.
 They are resistant to digestion or
denaturation and are insoluble in
 Hence majority of these proteins
have structural function.
 Examples are keratin in hair, skin
and nail; elastin in lungs;
collagen in bones; and myosin an
tropomyosin of the muscles.
 Shape is dominated by a single type
of secondary structure; usually α-
helix
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 B). Based on nutritional (biological) value

 Based on their nutritional value proteins can be classified as:

1. Complete (nutritionally rich) proteins - contain all the
essential amino acids.
Ex. casein of milk is a nutritionally rich protein.
2. Incomplete proteins - lack one essential amino acid for
example, cereal proteins lack lysine; and
3. Poor proteins - lack many essential amino acids. Ex, zein, a
corn protein lack tryptophan and lysine.

66
 C) Based on chemical composition

1) Simple proteins: contain only the amino acid residues.

Ex: Albumin, Globulins, protamines, histones, etc.

2) Compound or complex proteins: composed of a protein

and a non protein component (prosthetic group). The
protein component alone is called apoprotein.
 The apoprotein combined with the prosthetic group is
called holoprotein.
Ex: Glycoproteins, lipoproteins, Heme proteins like
hemoglobin and myoglobin, Metaloproteins,
Nucleoproteins, Chromoproteins.

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 Functions of proteins
 Some of the primary functions of proteins are listed here.
 Structural: Proteins are the main structural component in bone,
muscles, cytoskeleton and cell membrane.
 Nutrition: Provide the body with essential amino acids,
nitrogen and sulfur. Some glucogenic amino acids can be
converted to glucose.
 Catalytic: All metabolic enzymes are proteins in nature.
 Endocrine: Most hormones and all receptors are protein in
nature.
 Defense: The antibodies (immunoglobulins) and complement
system that play an important role in the body’s defensive
mechanisms are proteins in nature.
 Osmotic Potential: Plasma proteins are responsible for most
effective osmotic pressure of the blood. This osmotic pressure
plays a central role in many processes, e.g., urine formation.
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 Blood clotting factors are proteins.
 Transport role
 Lipoproteins carry lipids in the blood forming lipoprotein
complexes (chylomicron, VLDL, LDL,HDL).
 Proteins also carry, hormones, e.g., thyroid hormones and
minerals, e.g., calcium, iron and copper.
 Hemoglobin carries O2 from the lung to tissues is a protein.
 Membrane transport: The proteins in the membranes act as
channels or specific carrier proteins to allow selective
molecules/ions to cross into or out of the cells.
 Gene expression: Most factors required for DNA replication,
transcription and mRNA translation are protein in nature.
 Signal Transduction: Cell-environment, intercellular and
intracellular communication is carried out largely by proteins.
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