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Biomolecules Notes by Andleaf
Biomolecules Notes by Andleaf
Chapter : Biomolecules
BIOMOLECULES
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
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
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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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
NUCLEIC ACIDS
Polymer of Nucleotides
Each nucleotide comprises
↓ ↓ ↓
Sugar/ Hetrocyclic Phosphate
Monosaccharides Nitrogenous
Base
↓ ↓
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Nucleoside
↓
Nucleotide
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
1. O
||
O CH2 - O - C - R1
|| |
R2 - C -O - CH O
| ||
CH2 - O - C - R3
Triglyceride
(R1 , R2 , R3 are fatty acids)
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
* Non essential
* Essential
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
→2β
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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* 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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E + S ⇋ ES → EP → E + P
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~ Exothermic
P lower than S
~ Endothermic
S lower than P
(b) PH
~Highest activity at opt. PH
~Rate ↓↓ both below & above the optimum
(d) Inhibitors
~Competitive
~Inhibitor & substrate both compete for active site
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Classification
~ 6 classes each with 4-13 subclasses
(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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(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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