3 interactive concept widgets for Biomolecules. Drag any slider, change any number, and watch the formula and the answer update live. Built so you understand how each NEET problem actually works, not just the final number.
On this page
Compare the four classes of biomolecules: carbohydrate, protein, lipid and nucleic acid, with monomer, bonds, examples and functions.
Select any of the four biomolecule categories to explore its monomer, bond type, key examples, main biological functions and the NEET fact most often tested about it.
Feature
Carbohydrate
Protein
Lipid
Nucleic Acid
Monomer
Monosaccharide (e.g. glucose, fructose, ribose)
Amino acid (20 standard types, each with a unique R group)
Fatty acids + glycerol (not a true polymer)
Nucleotide (sugar + phosphate + nitrogenous base)
Bond type
Glycosidic bond (alpha or beta, 1-4 or 1-6)
Peptide bond (-CO-NH-) formed by condensation
Ester bond (in triglycerides and phospholipids)
Phosphodiester bond (3' to 5' between nucleotides)
Protein: examples and functions
Key examples
Main functions
NEET fact
RuBisCO is the most abundant protein in the biosphere. Collagen is the most abundant protein in animals. Haemoglobin (4 subunits) and collagen (3 chains) have quaternary structure.
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Walk through the four levels of protein structure: primary, secondary, tertiary and quaternary, with the bonds and an example at each level.
Click any of the four levels to see what defines it, the bonds that hold it together, example proteins and the NEET fact most often tested.
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Shape
A linear chain (like beads on a string). No 3D folding yet.
Example proteins
The sequence "Met-Ala-Gly-Val..." in a polypeptide chain. Even one amino acid change alters protein function. In sickle-cell anaemia, glutamate at position 6 of the beta-haemoglobin chain is changed to valine.
Primary Structure
What defines it
The linear sequence of amino acids from the N-terminus (free amino end) to the C-terminus (free carboxyl end). This sequence is directly coded by the DNA sequence of the gene.
Bonds involved
Peptide bonds (-CO-NH-) between adjacent amino acids. Formed by condensation (water released). Strong covalent bonds.
NEET fact
Primary structure is held by peptide bonds. Changing even one amino acid in the primary sequence can destroy protein function (e.g. sickle-cell anaemia).
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Drag the temperature and pH controls and watch enzyme activity rise to an optimum and then fall as the enzyme denatures.
Use the sliders to set temperature (0 to 80 degrees C) and pH (1 to 13). The bell curves show how activity changes, mark the optimum, and explain what happens past the optimum. Switch enzyme presets to compare a typical body enzyme, pepsin and a plant enzyme.
e.g. amylase, most human enzymes
Temperature: 37 °C
0 °C
Optimum: 37 °C
80 °C
pH: 7.0
pH 1 (acid)
Optimum: pH 7.4
pH 13 (base)
Overall enzyme activity: 95% (High)
Temperature effect: 100%
At optimum temperature
pH effect: 95%
NEET fact
Most human enzymes work best at body temperature (37 degrees C) and near-neutral pH (7 to 7.5). Above 40 degrees C, denaturation begins rapidly.
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Drag, slide and recompute on the next chapter's widgets.
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