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Biomolecules - Complete NEET Biology Notes 2026

Master Biomolecules for NEET 2026 with detailed notes on carbohydrates, proteins, lipids, nucleic acids, and enzymes. NCERT-aligned content with diagrams and previous year questions.

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Dr. Shekhar
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December 12, 2025
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Key Takeaways

  • 1Carbohydrates follow the formula Cn(H2O)n and are classified as mono-, di-, and polysaccharides
  • 2Proteins are polymers of amino acids linked by peptide bonds
  • 3Enzymes are biological catalysts that lower activation energy without being consumed
  • 4DNA is double-stranded, RNA is single-stranded - key structural differences
  • 5Lipids are hydrophobic molecules important for energy storage and membranes

Remember these points for your NEET preparation

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NCERT-aligned notes
Previous year questions
Expert tips

Biomolecules - Complete NEET Biology Notes

Biomolecules chapter contributes 4-6 questions in NEET and forms the foundation for understanding biochemistry. This guide covers all NCERT concepts essential for NEET 2026.

Introduction to Biomolecules

Living organisms are made up of various chemical compounds called biomolecules. These can be classified as:

CategoryExamplesCharacteristics
MicromoleculesSugars, amino acids, nucleotidesLow molecular weight, simple
MacromoleculesProteins, nucleic acids, polysaccharidesHigh molecular weight, polymers

Primary vs Secondary Metabolites:

  • Primary: Essential for life (amino acids, sugars, fatty acids)
  • Secondary: Not essential but provide ecological advantage (alkaloids, terpenes, pigments)

Carbohydrates

General Formula

Cn(H2O)n - hence the name "hydrates of carbon"

Classification

1. Monosaccharides (Simple Sugars)

SugarCarbon atomsExampleSource
Triose3CGlyceraldehydeGlycolysis intermediate
Tetrose4CErythrosePentose phosphate pathway
Pentose5CRibose, DeoxyriboseRNA, DNA
Hexose6CGlucose, Fructose, GalactoseMost common

Important Hexoses:

  • Glucose (dextrose/grape sugar): Blood sugar
  • Fructose (levulose): Sweetest natural sugar, found in fruits
  • Galactose: Component of lactose

2. Disaccharides

DisaccharideComponentsBondSource
SucroseGlucose + Fructoseα-1,2Sugarcane, beetroot
MaltoseGlucose + Glucoseα-1,4Germinating seeds
LactoseGlucose + Galactoseβ-1,4Milk

NEET Tip: Sucrose is a non-reducing sugar because both anomeric carbons are involved in the glycosidic bond.

3. Polysaccharides

PolysaccharideMonomerBond TypeFunction
Starchα-glucoseα-1,4 (amylose), α-1,4 & α-1,6 (amylopectin)Plant storage
Glycogenα-glucoseα-1,4 & α-1,6 (more branched)Animal storage
Celluloseβ-glucoseβ-1,4Plant cell wall
ChitinN-acetylglucosamineβ-1,4Fungal cell wall, exoskeleton

Key Difference: Starch and glycogen are digestible; cellulose is not (humans lack cellulase enzyme).


Proteins

Amino Acids - Building Blocks

General Structure:

  • Central carbon (α-carbon) attached to:
    • Amino group (-NH₂)
    • Carboxyl group (-COOH)
    • Hydrogen atom
    • R group (side chain) - determines properties

Classification by R Group:

TypePropertyExamples
Non-polarHydrophobicGlycine, Alanine, Valine, Leucine
Polar unchargedHydrophilicSerine, Threonine, Asparagine
AcidicNegatively chargedAspartic acid, Glutamic acid
BasicPositively chargedLysine, Arginine, Histidine
AromaticRing structurePhenylalanine, Tyrosine, Tryptophan

Essential Amino Acids (must be obtained from diet): Mnemonic - PVT TIM HALL

  • Phenylalanine, Valine, Tryptophan, Threonine, Isoleucine, Methionine, Histidine, Arginine, Leucine, Lysine

Peptide Bond

  • Formed by condensation reaction between -COOH of one amino acid and -NH₂ of another
  • Results in release of water
  • Partial double bond character (planar, rigid)

Protein Structure

LevelDescriptionBonds Involved
PrimaryLinear sequence of amino acidsPeptide bonds
Secondaryα-helix, β-pleated sheetHydrogen bonds
Tertiary3D foldingH-bonds, ionic, disulfide, hydrophobic
QuaternaryMultiple polypeptide chainsSame as tertiary

Examples:

  • Primary only: Insulin A & B chains (before folding)
  • Secondary: Keratin (α-helix), Silk fibroin (β-sheet)
  • Tertiary: Myoglobin (single chain, 3D)
  • Quaternary: Hemoglobin (4 subunits: 2α + 2β)

Lipids

Characteristics

  • Hydrophobic (water-insoluble)
  • Soluble in organic solvents
  • No true polymer structure

Classification

1. Simple Lipids

Fatty Acids:

TypeStructureExamplesProperty
SaturatedNo double bondsPalmitic, StearicSolid at room temp
UnsaturatedDouble bonds presentOleic (1), Linoleic (2)Liquid at room temp

Triglycerides (Fats & Oils):

  • Glycerol + 3 fatty acids
  • Fats: Saturated (animal origin)
  • Oils: Unsaturated (plant origin)

2. Compound Lipids

TypeComponentsExampleFunction
PhospholipidsGlycerol + 2 FA + PhosphateLecithinCell membrane
GlycolipidsLipid + CarbohydrateCerebrosidesCell recognition
LipoproteinsLipid + ProteinLDL, HDLLipid transport

3. Derived Lipids

  • Cholesterol: Precursor for steroid hormones, vitamin D
  • Steroids: Testosterone, estrogen, cortisol

Nucleic Acids

Nucleotide Structure

Nucleotide = Nitrogenous base + Pentose sugar + Phosphate group

Nitrogenous Bases:

Purines (Double ring)Pyrimidines (Single ring)
Adenine (A)Cytosine (C)
Guanine (G)Thymine (T) - DNA only
Uracil (U) - RNA only

Base Pairing Rules (Chargaff's Rules):

  • A pairs with T (2 hydrogen bonds) in DNA
  • A pairs with U in RNA
  • G pairs with C (3 hydrogen bonds)

DNA vs RNA

FeatureDNARNA
SugarDeoxyriboseRibose
BasesA, T, G, CA, U, G, C
StructureDouble-strandedUsually single-stranded
LocationNucleus, mitochondria, chloroplastNucleus, cytoplasm, ribosomes
FunctionGenetic information storageProtein synthesis

Types of RNA

TypeFunctionLocation
mRNACarries genetic codeNucleus → Cytoplasm
tRNATransfers amino acidsCytoplasm
rRNAComponent of ribosomesRibosomes

Enzymes

Definition

Biological catalysts that speed up reactions without being consumed.

Properties

  1. Highly specific (lock and key / induced fit)
  2. Increase reaction rate by lowering activation energy
  3. Not consumed in reaction
  4. Work optimally at specific pH and temperature
  5. Can be regulated

Classification (IUBMB)

ClassReaction TypeExample
OxidoreductasesOxidation-reductionDehydrogenases
TransferasesTransfer of groupsKinases
HydrolasesHydrolysisLipases, Proteases
LyasesNon-hydrolytic removalDecarboxylases
IsomerasesIsomerizationMutases
LigasesBond formation using ATPSynthetases

Factors Affecting Enzyme Activity

FactorEffect
TemperatureIncreases to optimum, then denatures
pHOptimal pH varies (pepsin: 2, trypsin: 8)
Substrate concentrationIncreases until saturation
Enzyme concentrationDirectly proportional
InhibitorsCompetitive or non-competitive

Enzyme Inhibition

TypeMechanismEffect on KmEffect on Vmax
CompetitiveBinds to active siteIncreasesUnchanged
Non-competitiveBinds elsewhereUnchangedDecreases

Co-factors and Co-enzymes

TypeNatureExamples
Prosthetic groupTightly boundHeme in hemoglobin
Co-enzymeLoosely bound, organicNAD⁺, FAD, Coenzyme A
Metal ionInorganicZn²⁺, Mg²⁺, Fe²⁺

Previous Year NEET Questions

Q1 (NEET 2023): Which of the following is a non-reducing sugar?

  • (a) Maltose
  • (b) Lactose
  • (c) Sucrose ✓
  • (d) Glucose

Q2 (NEET 2022): The most abundant protein in the animal world is:

  • (a) Keratin
  • (b) Collagen ✓
  • (c) Hemoglobin
  • (d) Insulin

Q3 (NEET 2021): Which of the following is an example of pyrimidine?

  • (a) Adenine
  • (b) Guanine
  • (c) Cytosine ✓
  • (d) None of the above

Q4 (NEET 2020): Competitive inhibitor of an enzyme:

  • (a) Decreases Km
  • (b) Increases Km ✓
  • (c) Does not change Km
  • (d) Increases Vmax

Q5 (NEET 2019): Essential amino acids are those which:

  • (a) Are synthesized in the body
  • (b) Must be provided in diet ✓
  • (c) Are non-essential for growth
  • (d) None of the above

Quick Revision Points

  1. Sweetest sugar: Fructose
  2. Blood sugar: Glucose
  3. Milk sugar: Lactose
  4. Storage polysaccharide: Starch (plants), Glycogen (animals)
  5. Structural polysaccharide: Cellulose (plants), Chitin (fungi)
  6. Most abundant organic compound: Cellulose
  7. Most abundant protein: Collagen (animals), RuBisCO (world)
  8. Saturated fats: No double bonds, solid
  9. Unsaturated fats: Double bonds, liquid
  10. DNA sugar: Deoxyribose (lacks -OH at 2' carbon)

FAQs

Q: Why is sucrose called a non-reducing sugar? A: In sucrose, both anomeric carbons (C1 of glucose and C2 of fructose) are involved in the glycosidic bond, so there's no free aldehyde or ketone group to reduce other compounds.

Q: What makes an amino acid essential? A: Essential amino acids cannot be synthesized by the human body in sufficient quantities and must be obtained from the diet. There are 9 essential amino acids for adults.

Q: Why do enzymes have optimal temperature and pH? A: Enzymes are proteins with specific 3D structures. Temperature and pH changes can alter hydrogen bonds and ionic interactions that maintain this structure. Beyond optimal conditions, the enzyme denatures and loses activity.

Q: What is the difference between DNA and RNA in terms of stability? A: DNA is more stable because: (1) deoxyribose lacks 2'-OH making it less reactive, (2) double-stranded structure provides redundancy, (3) thymine instead of uracil prevents deamination errors.

Q: Why is RuBisCO considered the most abundant protein? A: RuBisCO (Ribulose-1,5-bisphosphate carboxylase/oxygenase) is found in all photosynthetic organisms and makes up about 50% of leaf protein. Given the vast amount of plant biomass on Earth, it's the most abundant protein globally.

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