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Chapter : Biomolecules
BIOMOLECULES
~ All the carbon compounds that we get from living
tissues can be called Biomolecules. However , living
organism have also got inorganic elements & compounds in
them
CHEMICAL ANALYSIS
Living tissue
(Plant tissue/animal + Trichloroacetic acid
tissue/microbial paste) (CI,CCOOH)
↓ ↓
Filtrate (Acid soluble) Retentate (Acid
Roughly cytoplasmic Insoluble
Components
↓ ↓
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Inorganic Organic
• Water •M.wt - 18 to 800 Da
• Ions (eg: Na , k , Ca , Mg Monomeric form
PO , SO etc) Eg : Simple sugars
• Gases Nucleotides
Amino acids
↓
Organic Biomacromolecule
M.wt - 10,000 Da
Polymeric form
• Polysaccharide
• Nucleic acid
• Proteins
Lipids (Not a polymer)
↓
~Not strictly Biomacromolecules M.wt <800 Da
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~Cell membrane fragment form
~Vesicles which are not water soluble
ELEMENTAL ANALYSIS
~Elemental analysis gives elemental composition of living
tissue in the form of hydrogen , oxygen , chlorine , carbon
Weight
Living tissue →→→ Wet weight
Dry
Living tissue →→→Dry weight
All water evaporates
Burn
Dried living →→→→→→→→ ‘Ash’(contains only
tissue All carbon compounds inorganic elements)
Oxidise to CO2 & H2O
~Carbon & hydrogen with respect to other elements are
more in any living organisms than in earth's crust
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~Oxygen is the most abundant element in living
Organism
~Analytical techniques gives an idea about the molecular
formula & the probable structure of the compound
Table-9.1 A comparison of elements present in non-living
& living matter
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Table-9.2 A list of representative inorganic constituents
of living tissues
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METABOLITES (BIOMOLECULES)
Primary metabolite Secondary metabolite
~Identifiable function ~Not involved in primary
~Play known role in Metabolism
Physiological processes ~Seems to have no direct
Eg: Sugars, amino acid , Function in growth &
Lipids , nitrogen bases etc Development of
Organisms
~Many of them are
Useful to human
Welfare Eg: rubber ,
drugs , spices &
pigments. some have
Ecological importance
~Eg : Flavonoids , anti-
-biotics etc
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Table-9.3 Some secondary metabolites
Table-9.4 Average composition of cells
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Table-9.5 Some proteins and their functions
CARBOHYDRATES
↓ ↓
Monosaccharides/sugar Polysaccharide
Single unit ~Many units/long chain
of sugars unit linked
together by glycosidic
Bond formed by
Dehydration
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↓ ↓
Homopolysaccharide Heteropolysaccharide
~Same monomers units ~Different monomers
Units
Glycogen right end is reducing while left
End is non reducing
Starch hold in helical portion
Cellulose cannot hold , as no helical portion
Cotton fibre → Cellulose
Paper is made from plant pulp
NUCLEIC ACIDS
Polymer of Nucleotides
Each nucleotide comprises
↓ ↓ ↓
Sugar/ Hetrocyclic Phosphate
Monosaccharides Nitrogenous
Base
↓ ↓
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Nucleoside
↓
Nucleotide
~Ribose sugar & Uracil exist in RNA (Ribonucleic
acid)
~2' deoxyribose sugar & thymine exist in DNA
(Deoxyribonucleic acid) DNA & RNA function as genetic
material
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Figure-9.3 Various levels of protein structure
Figure-9.4 Cartoon showing : (a) A secondary structure
(b) A tertiary structure of proteins
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Figure-9.5 Diagram indicating secondary structure of
DNA
WATSON CRICK MODEL OF B-DNA
•DNA exists are double helix (secondary structure)
•Two polynucleotide strands are helically coiled around a
common axis
•Two polynucleotide strands are antiparallel , run in
opposite direction & Complementary to each other.
•A & G of one strand compulsory base pairs with T & C
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respectively on the other strand
•Always two hydrogen bonds exist between A & T & three
hydrogen bonds between C & G
•Phosphate moiety links 3 carbon of one sugar of one
nucleotide to 5 carbon of sugar of succeeding nucleotide
•Nitrogen bases are perpendicular to backbone & faces
inside
•At each step of ascent , strand turns 36 degrees
1 turn = 10 base pairs
1 complete turn = 34A
Rise per base pair = 3.4A
LIPIDS
~Water insoluble
~Simple fatty acid
R-COOH (R→methyl , ethyl or Higher
form 1 to 19 carbon)
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TYPES
Saturated Unsaturated
No.of C=C • × • One or more
Double
bonds :
Example : • Palmitic acid • Arachidonic acid
(16 carbon (20 carbon
Including carboxyl Including
Carbon) Carboxyl)
CH3-(CH2)14-COOH
* Esters of fatty acids & Glycerol
No. Of fatty acids Glycerol
Mono 1 1
Di 2 1
Tri 3 1
↓ M.P Winter's state Eg
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Fats Higher Solid Ghee , butter
Oils Lower Liquid Gingeliy. Oil
1. O
||
O CH2 - O - C - R1
|| |
R2 - C -O - CH O
| ||
CH2 - O - C - R3
Triglyceride
(R1 , R2 , R3 are fatty acids)
2. Lipids have phosphorous & phosphorylated
organic comp. Called phospholipids
Eg : Lecithin ( found in cell membrane )
3. Cholesterol (Have lipid like properties)
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AMINO ACIDS
~Have amino group & acidic group on same carbon
i.e α - Carbon called α - Amnio acid
~Substituted methane
~Chemical & physical properties of amino acids are of
amino , Carboxyl & R-functional groups
TYPES
* On the basis of R-group
R-group Amino acids
-H Glycine
-CH3 Alanine
(Methyl)
-CH2-OH Serine
(Hydroxyl methyl)
On the basis of body req.
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* Non essential
* Essential
On nature of amino acids
Amino acids
Acidic → Glutamic acid
Basic → Lysine
Neutral → Valine
Aromatic → Tyrosine
Tryptophan
Phenylalanine
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Zwitterion
~ Insoluble group of -NH2 & -COOH
~Structures change with changing PH
R
|
H3N(+) - CH - COOH
↓↑
R
| (Zwitterionic
H3N+ - CH - COO(-) form)
↓↑ ↓
R Both +ive &
| -ive charge
H2N - CH - COO(-)
STRUCTURE OF PROTEINS
* Heteropolymer
* Peptide bonds (By dehydration)
* 20 types participate in formation
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Tertiary
↑
Primary ← Types → Secondary
↓
Quaternary
(a) Primary 1) As rigid rod
2) Provides positional information
(b) Secondary 1) Folded in the form of Helix
2) alpha-Helix , Beta-Helix
3) Right handed helices
(c) Teritary 1) 3-D
2) Most important for biological
Activities
(d) Quaternary1) More than one polypeptide chains
Hb→2α
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→2β
2) How individuals polypeptide
arranged W.R.T each other Proteins
Functions
• Collagen Intercellula ground sub.
• Trypsin Enzyme
• Insulin Hormone
• Antibody Fights Infections agents
• Receptor Sensory reception
• GLUT - 4 Enable , glucose transport into
Cells
Collagen : Most abundant in animal world
Rubisco : Most abundant in whole biosphere
Dynamic State
~Living →Non equi. Steady state (to be able to
State Perform work)
↓
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Or metabolism
↓
Sum of all reactions in Body.
* Not catalysed metabolic conversion
METABOLIC PATHWAY
↓ ↓
Catabolic Anabolic
~Degradation. ~Biosynthetic
~Complex to simple ~Simple to complex
~Energy released ~Energy used
Anaerobic
Eg : glucose →→→ lactic Eg : 1. Acetic acid
acid ↓
(Skeletal Cholesterol
muscles) 2. Amino acid
↓
Proteins
Glucose
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Glycolysis ↓ aerobic
Pyruvic acid
Glucose
↓ Anaerobic
Ethanol (yeast)
Carbonic
CO2 + H2O →→→→→ H2CO3
←←←←←
Anhydrase
↓
+ In cytoplasm
* Wtih enzyme → 6 lakh molecules of H2CO3
in 1 sec.
Rate → ↑↑ to million times
→ Without enzyme → 200 molecules / hour
Rate (dp/dt)
~Doubles or decrease by half for every 10°C
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changes in entire direction
* One biomolecule
↓ Turnover
Another biomolecule
ENZYMES (Biocatalyst)
Tertiary structure
Unchanged in the end
Highly specific
Not used during reaction
Generally proteinaceous except
Ribozymes (Nucleic acids)
6. ↑↑ rate by lowering activation energy
7. Have active sites/pockets to bind substrate
Inorganic catalyst
↓
~Work efficiently at high temperature & high pressure
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~Enzymes →Denatures at high temperature (>40°C)
~Thermophiles enzymes can tolerate
Substrate → Bind at active site of enzyme (E)
(S) ↓
ES complex
(Transient phenomenon)
↓
EP complex
↓
E+P
E + S ⇋ ES → EP → E + P
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Figure-9.6 Concept of activation energy
~ Exothermic
P lower than S
~ Endothermic
S lower than P
Factors effecting enzymes
(a) Temperature
~Highest activity at Opt. Temp.
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~Activity ↓↓ both below & above opt.
~Law temperature → Temporarily inactive
~High Temperature → Denaturating st.
(b) PH
~Highest activity at opt. PH
~Rate ↓↓ both below & above the optimum
Figure-9.7 Effect of change in : (a) PH (b) Temperature
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(c) Substrate concentration
~Initially , rate - ↑↑ with
Substrate concentration ↑↑
~Becomes constant →all enzyme get saturated
Concentration of substrate on enzyme activity
(d) Inhibitors
~Competitive
~Inhibitor & substrate both compete for active site
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~Both resembles in structure
~Eg (1) Succinic dehydrogenase by malonate
(2) Control of bacterial pathogens by
competitive inhibitors
Classification
~ 6 classes each with 4-13 subclasses
(1) Oxidore Ductase / Dehydrogenase
S reduced + S' Oxidised
↓
S oxidised + S' reduced
(2) Transferase
Transfer of gp (other than H)
S - G + S' → S + S' - G
(3) Hydrolases
Hydrolysis of ester , ether , peptide , glycosidic ,
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C-C , C-halide or P-N bonds.
(4) Lyases
Leave double bonds
X Y
| |
C - C → X-Y + C=C
(5) Isomerases
Inter conversion of optical , geometric or positional
isomers
(6) Ligases
Linking 2 compounds
Eg : Joining of C-O , C-S , C-N , P-O bonds
Enzymes
↓ ↓
Simple enzyme Confugated enzyme
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Only protein ↓ ↓
Apo-enzyme Co-factor
(Inactive)
~Protein part ~Non protein
Part
Catalytically active enzyme
Co - Factor
(No catalysis without this)
↓ ↓ ↓
Prosthetic Gp. Co-enzyme Metal ions
•Organic •Organic •form
•Tightly bound •Loosely bound Coordination
•Eg : Haem for •Eg : NAD Bonds
Catalase & NADP •Zn2+ for
Peroxidase Carboxypeptidase
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