NCERT Based KT’s PowerNotes

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Biomolecules
• G.N. Ramachandran: triple helical structure of collagen
• Linus Pauling: explained α-helix and β-sheet structures
• The concepts and techniques of physics and chemistry are
applied to understand biology. This Physico -chemical approach
to study and understand living organisms is called ‘Reductionist
Biology’.
Components of Living organism

How to find organic component of living organism?

Amino acids
Take living tissue → grind it in trichloroacetic acid → strain • Amino acids are called as α-amino acids.
through cotton → you get filtrate (acid-soluble pool) and retentate • They are substituted methane
or the (acid-insoluble fraction). • Made up of hydrogen, carboxyl group, amino group and a
Acid soluble pool (Filtrate) Acid insoluble pool (retentate) variable group designated as R group.
Low Molecular weight High Molecular weight • Around 20 types of amino acids are found in proteins
(18 – 800 Dalton) (Molecular weight More than 10000 Dalton)
Biomicromolecules Biomacromolecules R group Amino acid
Sugar, amino acids, Nucleotides, ions Carbohydrate, Proteins. Nucleic acid Hydrogen Glycine
Represent cytoplasmic composition Represent cytoplasmic + cell organelle composition Methyl group Alanine
hydroxy methyl Serine
• Weight of lipids do not exceed 800 Da, still considered as
macromolecule because lipids form vesicles in acid insoluble
• Nature of amino acids
pool
 Acidic amino acids →Glutamic acid
• Composition of cell :
 Basic amino acid → Lysine Uska basic loose hai
Water (70%) > Protein (10%) > Carbohydrates (3%) > Lipids (2%)
 Neutral amino acid → Valine
 aromatic amino acids → tyrosine, phenylalanine, tryptophan
How to find inorganic components of living organism?
• Zwitter ions PT karneka try karo aroma niklega
Destructive method  A particular property of amino acids is the ionizable nature of
–NH2 and –COOH groups. Hence in solutions of different
Take living tissue (e.g. leaf) → dry it : water evaporates → burn it
pH, the structure of amino acids changes. Under neutral
→ carbon compounds gets oxidised to gaseous form → ash
conditions, the amino acid will exist in its zwitterion form. A
contains inorganic elements (like calcium) → do analysis
zwitterion is a molecule that contains both a positive and a
negative charge, ph is called isoelectric pH
Carbohydrates • Essential amino acids
 amino acids which are essentially supplied through our diet
Cellulose
are called essential amino acids
• Homopolymer i.e., polysaccharide consisting of only one type of
• Non-essential amino acids
monosaccharide e.g., Glucose
 These are amino acids that body can make
• Found in cell wall of plant, algae
• Cellulose is the most abundant organic polymer on Earth.
Proteins
• Ruminants can digest cellulose
• Proteins are polypeptides.
• Microbes in ruminants have Cellulase enzyme
• They are linear chains of amino acids linked by peptide bonds
• Humans can’t digest cellulose
• Protein is a heteropolymer and not a homopolymer
• Paper pulp uses cellulose
• Collagen is the most abundant protein in animal world
• Ribulose bisphosphate Carboxylase-Oxygenase (RuBisCO) is
Starch
the most abundant protein in the whole of the biosphere.
• store house of energy in plant tissues
• Starch forms helical secondary structures. Protein Functions
• Starch can hold I2 molecules in the helical portion. Collagen Intercellular ground substance
• The starch-I2 is blue in colour. Trypsin Enzyme
Antibody Fights infectious agents
Glycogen Receptor Sensory reception (smell, taste, hormone, etc.)
• store house of energy in animal tissues GLUT-4 Enables glucose transport into cells

Inulin Structure of proteins Isko mat bhulna

• polymer of fructose Primary structure Amino acids linked with each other to form thread like structure
Secondary structure The amino acid thread, fold upon itself to form alpha helix and beta
Chitin pleated sheet. In proteins, only right-handed helices are observed
• Chitin is a complex polysaccharide Tertiary structure Three-dimensional folding pattern where protein thread is folded upon
• Homopolymer of N acetyl Glucosamine itself (like a hollow woollen ball) with the help of hydrogen and
• Forms exoskeleton of insect and fungi disulphide bond. Tertiary structure is absolutely necessary for the
many biological activities of proteins
Quaternary structure Protein consisting of more than one amino acid chain
In a polysaccharide chain (say glycogen), the right end is called e.g., Haemoglobin
the reducing end and the left end is called the non-reducing end.
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 NCERT Based KT’s PowerNotes
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Glycerol

• Glycerol is trihydroxy propane

• Many lipids have both glycerol and fatty acids. Here the fatty
acids are found esterified with glycerol

Phospholipid
• Phospholipids have phosphorous in them
• E.g., Lecithin: major component of bilayer cell membrane
• Sphingolipid: found in myelin sheath of nervous cells

Primary and secondary metabolites Bonds in Polymers

• Primary metabolites
 Primary metabolites are molecules which have identifiable Polymer Monomer Bonds in monomer
functions and known roles in normal physiological processes, Polysaccharide Monosaccharide Glycosidic bonds
 e.g., amino acids, sugars, etc. Proteins Amino acids Peptide Bonds
• Secondary metabolites DNA Nucleotides Phospodiester bonds
 Secondary metabolites are molecules produces by plant,
Lipid Lipid is not a polymer
fungal and microbial cells whose role or functions are not
known.
Dynamic state of body constituents
Nucleic acid • The metabolic pathway includes a series of reactions. The
• DNA is a macromolecule metabolite flow, the rate, and direction at which metabolism
• Nucleic acids exhibit secondary structures takes place are called the dynamic state of body constituents.
• DNA double helix model was proposed by Watson and Crick • All metabolic reactions are catalysed by a set of proteinaceous
• DNA is a polymer of nucleotide compounds called enzymes.
• Nucleotides is made up of 3 components: monosaccharide, • Anabolic pathways:
Phosphoric acid or phosphate and heterocyclic compound  Simple structure form complex structure
• Heterocyclic ring is Purine (Adenine and Guanine) and  Consumes energy
Pyrimidines (Cytosine, thymine, uracil)  E.g., acetic acid becomes cholesterol
• Each strand appears like a helical staircase. • Catabolic pathway:
• At each step of ascent, the strand turns 36°.  Complex structure leads to simpler structure
• One full turn of the helical strand - ten base pairs.  Releases energy
• The pitch = 34Å.  E.g., Glucose becomes lactic acid in our skeletal muscle
• The rise per base pair = 3.4Å. This
• B-DNA is the term given for the right-handed DNA helix that Anabolism means constriction & catabolism means destruction
is the most common form of DNA
The living state
DNA bonds • The living state is a non-equilibrium steady-state to be able to
Pentose sugar + Nitrogen base: Nucleoside perform work.
Nucleoside + Phosphate group: Nucleotide • The living process is a constant effort to prevent falling into
5’ end = free phosphate group equilibrium and is achieved by energy input. The metabolism
N Glycosidic provides a mechanism for the production of energy.
bond
3’ end = free OH group
• The living state and metabolism are synonymous, without
RNA
Sugar: Ribose sugar (- OH group at 2’ C)
metabolism there cannot exist a living state.
Phospoester bond Uracil in place of thiamine (5 Methyl Uracil) • A living organism works continuously so it cannot
afford to reach equilibrium because a system at equilibrium
cannot perform the work
Nucleoside Nucleotides
Adenosine Adenylic acid
Enzymes
Guanosine Thymidylic acid
Thymidine Guanylic acid
• Almost all enzymes are proteins
Uridine Uridylic acid • Except ribozyme which is a nucleic acid (RNA)
Cytidine Cytidylic acid • The Globular tertiary structure enables proteins to function as
enzymes.
• An active site of enzyme is a pocket into which the substrate fits
Lipids • Difference between Enzyme catalysts and inorganic catalysts
• Lipids are: fatty acids, glycerol and phospholipids  Inorganic catalysts work efficiently at high temperatures and
high pressures, while enzymes get damaged at high
Fatty acids
temperatures
• A fatty acid has a carboxyl group attached to an R group
• Carbonic anhydrase enzyme (found in RBC and Plasma)
• Palmitic acid has 16 carbons, Arachidonic acid has 20 carbon
accelerates the below reaction rate by about 10 million times
• Types
 Saturated Fatty acids: no double bond
 Unsaturated fatty acids: have one or more C=C double bonds

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Mechanism of enzyme action Classification and Nomenclature of Enzymes
• Enzyme bring out chemical and physical changes in substrate Enzymes are divided into 6 classes each with 4-13 subclasses and
• Enzyme substrate complex is a transient state named accordingly by a four-digit number. OT HILL
• In both exothermic and endothermic reaction, the ‘S’ has to go
through a much higher energy state or transition state means Oxidoreductases/dehydrogenases: Enzymes which catalyse
substrate needs to be activated by energy called as activation oxidoreduction between two substrates S and S’ e.g.,
energy
• Activation energy is needed in both Endothermic and exothermic
reaction Transferases: Enzymes catalysing a transfer of a group, G (other
• Role of enzyme in reactions is to decrease activation energy than hydrogen) between a pair of substrate S and S’ e.g.,

Hydrolases: Enzymes catalysing hydrolysis of ester, ether,

The catalytic cycle of an enzyme action can be described in the peptide, glycosidic, C-C, C-halide or P-N bonds.
following steps:
1. First, the substrate binds to the active site of the enzyme, Isomerases: Includes all enzymes catalysing inter-conversion of
2. Enzyme alter its shape and fit more tightly around the substrate. optical, geometric or positional isomers.
3. Enzyme breaks the chemical bonds of the substrate
4. The enzyme releases the products of the reaction and Ligases: Enzymes catalysing the linking together of 2 compounds,
5. The free enzyme is ready to bind to another molecule of the e.g., enzymes which catalyse joining of C-O, C-S, C-N, P-O etc.
substrate bonds.

Factors Affecting Enzyme Activity Lyases: Enzymes that catalyse removal of groups from substrates
(1) Temperature and pH (2) substrate concentration by mechanisms other than hydrolysis leaving double bonds
(3) binding of specific chemicals

(1) Temperature and Ph Co-factors

• Each enzyme shows its highest activity at a particular • Enzymes are composed of one or several polypeptide chains
temperature and pH called the optimum temperature and • However, there are a number of cases in which non-protein
optimum pH constituents called cofactors are bound to the enzyme to make
• Activity declines both below and above the optimum value. the enzyme catalytically active
• Low temperature → preserves enzyme in a temporarily inactive • Catalytic activity is lost when the co-factor is removed from the
state enzyme
• high temperature → destroys enzymatic activity because proteins • The protein portion of the enzymes is called the apoenzyme
are denatured by heat. • Three kinds of cofactors may be identified: prosthetic groups,
co-enzymes and metal ions.

✓ Km is Substrate conc at which enzyme velocity is half of Vmax

✓ Vmax is the maximum velocity of the reaction for the given
concentration of enzyme.

(2) Concentration of Substrate

With the increase in substrate concentration, the velocity of the
enzymatic reaction rises at first. The reaction ultimately reaches a
maximum velocity (Vmax) which is not exceeded by any further
rise in concentration of the substrate
Inhibitor non competitive bhi ho -------------------------------------END-------------------------------------
(3) binding of specific chemicals sakta hai par NCERT ne competitive
competitive inhibitor inhibitor hi aapko bataya hai
• closely resembles the substrate [Link]
• competes with substrate for substrate binding site of the enzyme
• Consequently, the substrate cannot bind and as a result, the
enzyme action declines
• e.g., inhibition of succinic dehydrogenase by malonate which
closely resembles the substrate succinate in structure.
• Such competitive inhibitors are often used in the control of
bacterial pathogens e.g., Penicillin, for example, is a competitive
inhibitor that blocks the active site of an enzyme that many
bacteria use to construct their cell wall
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