BIOMOLECULES
Chemical compounds found in living organisms.
INORGANIC BIOMOLECULES ORGANIC BIOMOLECULES
includes minerals, gases and includes carbohydrates, fats,
water. proteins, nucleic acids,
vitamins, etc.
• CHEMICAL FORMS OF • BIOCHEMICAL FORMS
BIOMOLECULES: OF BIOMOLECULES:
Aldehyde, Ketones The Amino Acids,
and Aromatic Nucleotides and Fatty
Compounds. Acids.
ANALYSIS OF CHEMICAL COMPOSITION IN A TISSUE
• Grind a living tissue (a vegetable or a piece of
liver, etc.) in trichloroacetic acid (Cl3CCOOH) to
obtain a thick slurry.
• Strain this through a cheesecloth or cotton to
obtain two fractions as filtrate or more
technically, the acid-soluble pool, and the
second, the retentate or the acid-insoluble
fraction.
FILTRATE (acid soluble pool) 2. RETENTATE (acid insoluble pool)
Contains Bio-macromolecules having Molecular
• Contains Bio-micromolecules having
Molecular Weight is less than 1000 Daltons. Weight is greater than 1000 Daltons.
BIOMICROMOLECULES INCLUDE:
AMINO ACIDS
LIPIDS
NITROGENOUS BASES
SUGARS
BIOMACROMOLECULES INCLUDE:
PROTEINS
POLYSACHHARIDES
NUCLEIC ACIDS
ANALYSIS OF INORGANIC COMPOUNDS
Weigh a living tissue (wet
weight) and it is dried (dry
weight) to evaporate water.
It is fully burnt to oxidize all
carbon compounds to gaseous
form (CO2 & water vapour). It
forms ash.
Then ash contains inorganic
elements like Ca, Mg, Na, K, etc.
and inorganic compounds like
sulphates, phosphates, NaCl,
CaCO3 , etc.
ANALYSIS OF ELEMENTS IN LIVING AND NON-LIVING
MATTER
T ES
D R A
H Y
R B O
C A
CARBOHYDRATES
• Carbohydrates consist of carbon,
hydrogen, and oxygen.
• The general empirical structure for
carbohydrates is (CH2O)n.
• They are the most abundant organic
molecules in nature and also referred to as
“saccharides”.
• The building blocks of all carbohydrates are
simple sugars called monosaccharides.
CLASSIFICATION OF CARBOHYDRATES
SIMPLE SUGARS
• Sugars are sweet and water soluble carbohydrates.
• They are formed by C, H and O in the ratio of 1:2:1
• e.g., Glucose Ribose, etc.
POLYSACCHARIDES
These are polymers of monosaccharides (Simple sugars)
STARCH
• It is a homopolymer of glucose
CELLULOSE
• It is a homopolymer of glucose
GLYCOGEN
It is a homopolymer of glucose
INULIN
• It is a homopolymer of fructose
ID S
AC
I N O
A M
AMINO ACIDS
• They are the compounds formed of an amino group
(-NH2), a carboxylic acid group (-COOH), hydrogen
(H) & a variable group (R).
• -NH2 & -COOH are attached to the same carbon atom
(α-carbon). So, they are called α-amino acids. They
are substituted methanes.
• Based on the nature of R group there are many
amino acids. However, those which occur in proteins
are only of twenty types.
20 TYPES OF AMINO ACIDS ARE USED IN PROTEIN SYNTHESIS
FEW EXAMPLES OF PROTEINACEOUS AMINO ACIDS
GLYCINE ALANINE SERINE
R is a R is a R is a
hydrogen methyl hydroxy
atom group methyl
group
TYPES OF AMINO ACIDS
ACIDIC AMINO ACIDS
e.g. Glutamic acid
BASIC AMINO ACIDS
e.g. Lysine
NEUTRAL AMINO ACIDS
e.g., Valine
Some amino acids are aromatic e.g., Tyrosine, Phenyl alanine, Tryptophan
• In amino acids, amino group (-NH2) and carboxylic acid group (-COOH) have
ionizable nature. So, structure of amino acids changes in solutions of different
pH.
• If both amino group (-NH2) and carboxylic acid group (-COOH) are ionized, it is
called Zwitter Ion.
I D S
L I P
Lipid is a micro-molecule as its
molecular weight does not exceed
800 Da. But it comes under acid
insoluble fraction because many
lipids are arranged into structures
like cell membranes. When a tissue
is grinded, cell membranes are
broken and form water insoluble
vesicles. They cannot be filtered
along acid soluble fraction.
LIPIDS
❑Water insoluble.
❑Contain C, H & O
but number of
oxygen atoms is less.
TYPES OF LIPIDS
SIMPLE LIPIDS
COMPOUND
LIPIDS
DERIVED LIPIDS
TYPES OF LIPIDS
SIMPLE LIPIDS
• These are formed of Fatty acids & alcohol like
glycerol.
• Fatty acids are lipids with a hydrocarbon chain (R-
group) ending in –COOH group i.e., R-COOH.
• E.g., Palmitic acid has 16 carbons (CH3-(CH3)14-COOH
or C15H11-COOH) and Arachidonic acid has 20
Carbons.
TYPES OF FATTY ACIDS
SATURATED FATTY ACIDS UNSATURATED FATTY ACIDS
• They have no double or triple bonds
• They have one or more double bonds
between carbon atoms.
between carbon atoms.
• E.g, Palmitic acid
• E.g, Oleic acid (C17H33COOH)
Stearic acid (C17H35COOH)
Arachidonic acid (C19H31COOH)
STRUCTURE OF GLYCEROL (trihydroxy propane)
Fatty acids are
esterified with glycerol
through ester bond
forming
monoglycerides,
diglycerides &
triglycerides.
1 glycerol + 1 fatty acid Monoglyceride
1 glycerol + 2 fatty acid Diglyceride
1 glycerol + 3 fatty acid Triglyceride
TRIGLYCERIDES
Based on melting point, Lipids
(triglycerides) are of 2 types:
❑Fats: Higher melting point
❑Oils: Lower melting point.
COMPOUND LIPIDS
• These are the esters of fatty acids and alcohol with additional groups.
• E.g., Phospholipids (fatty acids + glycerol + phosphate). They are found in cell membranes.
• E.g., Lecithin
DERIVED LIPIDS
• These are the products of hydrolysis of simple lipids and compound lipids.
• E.g., Cholesterol.
IN S
OT E
P R
• Proteins are heteropolymer of amino acids.
• They are polypeptides, i.e., linear chains of amino acids linked by peptide bonds.
• Peptide bond is formed when –COOH group of one amino acid reacts with –NH2 group of next
amino acid by releasing a molecule of water (dehydration).
For growth and repair
FUNCTIONS
OF Transport nutrients across cell membranes.
E.g. GLUT-4 enables glucose transport into cell.
PROTEINS
Acts as intercellular ground substance.
Eg: Collagen
Acts as antibodies to fight infectious organisms.
Acts as receptors.
Eg: receptors of smell, taste, hormones.
Some are hormones (e.g. Insulin), enzymes (e.g. trypsin), pigments
(e.g. hemoglobin) etc.
MOST ABUNDANT PROTEIN IN MOST ABUNDANT PROTEIN IN
ANIMAL WORLD THE BIOSPHERE
It’s one of the major building blocks of bones, skin, RubisCo- Ribulose-1,5- biphospahte.
muscles, tendons, and ligaments. Collagen is also It is crucial for carbon fixation and source of energy
found in many other body parts, including blood for all heterotrophs.
vessels, corneas, and teeth.
STRUCTURAL LEVELS OF PROTEIN
❑PRIMARY STRUCTURE
❑SECONDARY STRUCTURE
❑TERTIARY STRUCTURE
❑QUATERNARY STRUCTURE
PROTEIN - PRIMARY STRUCTURE
• It describes the sequence of amino acids, i.e., positional information in a
protein.
• Left end: First amino acid (N – terminal amino acid)
• Right end: Last amino acid (C – terminal amino acid)
PROTEIN - SECONDARY STRUCTURE
• Here, one or more polypeptide
chains are folded in the form of a
helix or sheet, which are
stabilized by hydrogen bonds.
• It has only right-handed helices.
• E.g. Keratin, Fibroin (Silk Fibre).
EXAMPLES OF PROTEIN - SECONDARY
STRUCTURE
PROTEIN - TERTIARY STRUCTURE
Here, helical polypeptide chain is further folded like a hollow woolen ball.
It gives 3-D view.
Tertiary structure is necessary for many biological activities of proteins.
e.g. Myoglobin, Enzymes.
PROTEIN - QUATERNARY STRUCTURE
Here, more than one polypeptide chains form tertiary structure and each chain
functions as subunits of protein.
E.g. Haemoglobin. It has 4 subunits (2 α sub-units and 2 β sub-units).
ENZYMES
Name some of the
enzymes present in human
digestive system.
PEPSIN, SALIVARY
AMYLASE, TRYPSIN,
LIPASE
What are enzymes?
HUMAN DIGESTIVE SYSTEM
ENZYMES
• Protein catalysts.(What are
catalysts?)
• Facilitate biochemical reactions
inside the body of living
organisms.
• They lower the activation
energy for a reaction.(Input
energy required to start a
reaction)
Role of enzymes in Chemical reactions
RUSTING OF IRON
CURDLING OF MILK
Role of enzymes in metabolic reactions
RESPIRATION PHOTOSYNTHESIS
Discovery
▪ Enzymes were discovered
accidentally by a British chemist
,EDUARD Buchner
▪ The term was coined by Kuhne.
▪ Enzyme means yeast in Greek.
Are all enzymes proteins?
ENZYMES…CONT
• Mostly enzymes are proteins.
• Some nucleic acids behave like enzymes, called
RIBOZYMES.
RIBOZYME
PROTEIN ENZYMES
• SIMPLE PROTEIN ENZYMES
Enzymes which are only proteins.
• HOLOENZYMES
Conjugated protein enzymes.
Enzymes with a non-protein group tightly bound
(prosthetic grp)
to a protein group.
(apoenzyme)
Enzymes: Characteristics
• Proteinaceous
- Simple/ conjugate
• Structure
-3-dimensional structure
-Substrate –binding sites are
present
• Solubility
Mostly water soluble
Some are water insoluble
• Catalytic behaviour
-Increases rate of reaction
-Remain unaltered during a chemical reaction
Enzymes: naming
• Enzymes are named after compounds / class they
act.
• Names end with ase
For example: Maltose MALTASE Glucose +Glucose
Working of enzymes
• SUBSTRATE
-Reactants on which enzymes act.
• PRODUCT S+ E P
-Result of the reaction
• ACTIVE SITE
-Region of the enzyme with a corresponding shape where the
substrate can fit in.
-Substrate binding site
Mechanism of Enzyme Action
LOCK AND KEY HYPOTHESIS
▪ First postulated by Emil Fischer.
▪ The lock is the enzyme and key is the substrate.
▪ Only the correctly sized key(substrates) fits into the key
hole (active site) of the lock (enzyme)
Mechanism…CONT.
INDUCED FIT HYPOTHESIS
Factors affecting Enzyme activity
• Temperature
• pH
• Enzyme concentration
• Substrate concentration
Factors: Temperature
Enzymes are most active at an optimum temperature
( 370C in humans).
Show little activity at low temperature
At high temperature lose activity due to denaturation.
Factors: pH
Rate of all enzymes catalysed reactions
depend on pH
Most enzymes exibit optimal activity at pH
value 5 to 9.
Factors: Enzyme concentration
As the concentration of enzyme increases
the rate of reaction will also increase.
FACTORS: Substrate Concentration
Increasing substrate concentration also increases the rate
of reaction upto a certain point
Once all the enzymes have bound, concentration increase in
substrate will have no effect on the rate of reaction as the
available enzymes will be saturated and working at their
maximum rate.