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Short notes of biomolecules.

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  • October 1, 2023
  • 11
  • 2021/2022
  • Interview
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  • Secondary school
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Biomolecules

• Carbon & hydrogen are more in living organism than earth's crust.

How to analyse chemical composition?

• Grind living tissue in trichloroacetic acid using mortar & pestle.
• Strain thick slurry through cheesecloth.
• One is filterate (acid soluble) & other retentate (acid insoluble).
• For inorganic: Dry small amount of living tissue, water evaporates & remaining material
gives dry weight. If its fully burnt, carbon compounds oxidise & ash remains.
Ash - inorganic elements (Calcium, Magnesium etc.)
• Biomolecules- All carbon compounds we get from living tissues.

Primary & Secondary Metabolites
Primary: For growth & metabolism, physiological process.
Secondary: Not used for growth. Eg: alkanoids, rubber, spices etc. Used for commercial
purpose.

Table: Some secondary metabolites

Pigments Carotenoids, Anthocyanins, etc.
Alkaloids Morphine, Codeine, etc.
Terpenoides Monoterpenes, Diterpenes, etc.
Essential oils Lemon grass oil, etc.
Toxins Abrin, Ricin
Lectins Concanavalin A
Drugs Vinblastin, curcumin, etc.
Polymeric substances Rubber, gums, cellulose


Biomacromolecules:

• Acid soluble: Weight from 18-800 daltons (Da), micromolecules. Eg: inorganic compounds
- sulphate, phosphate.
• Acid insoluble: 10000 dalton or above, biomacromolecules. Eg: polysachharide, lipid,
nucleic acid, proteins.

Table: Average composition of cells

Component % of the total cellular mass
Water 70 – 90
Proteins 10 – 15
Carbohydrates 3
Lipids 2
Nucleic acids 5–7

, Biomolecules
Ions 1
But lipid don't weigh more than 800 Da, as they separate in form of vesicles.
• Water is the most abundant chemical in living organism.

Proteins: Linear chain of amino acid linked by peptide bonds.
• Polypeptide, heteropolymer of amino acid (20 types of amino acid).
• Homopolymer - only 1 type of monomer repeating n no.of times.
• GLUT-4 transport glucose.
• 2 types of amino acid-
→ Essential: Not synthesised in body, outsourced.
→ Non-essential: Synthesised in body, need not be outsourced.
• Transport nutrients, fight infectious organism
• Some are hormones (insulin), some are enzymes (trypsin)
• Amino acid have amino group + acidic group on same carbon. i.e. α – carbon. So, called α-
amino acid (substituted methane)
• 4 substituent groups- Hydrogen, carboxyl group, amino, R (variable)
• If R is hydrogen, amino acid is called glycine, if methyl then amino acid is alanine, if
hydroxyl methyl then amino acid is Serine.




• They can be-
Acidic: Glutamic acid
Basic: Lysine
Neutral: Valine
•Aromatic amino acid- tyrosine, tryptophan, phenylalanine.
•Ionisable nature of –NH2 & -COOH makes amino acid – Zwitter ion. So, their structure
differ at different pH.
*Collagen is most abundant protein in animal world.
* RUBISCO is most abundant protein in whole biosphere.

Table: Some proteins and their Functions
Protein Functions
Collagen Intercellular ground substance
Trypsin Enzyme
Insulin Hormone
Antibody Fights infectious agents
Receptor Sensory reception (smell, taste,
hormone, etc.)
GLUT – 4 Enables glucose transport into cells

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