NEET (UG)

Biomolecules

Carbohydrates, proteins, nucleic acids, vitamins and hormones for NEET

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Module 1

Carbohydrates and Proteins

Carbohydrates: Classification and StructureTopic 1

Carbohydrates are optically active polyhydroxy aldehydes or ketones, or compounds that produce them on hydrolysis. They are the most abundant biomolecules, providing energy (glucose), storage (starch, glycogen) and structure (cellulose). They are classified by how many simple sugar units they give on hydrolysis: monosaccharides cannot be hydrolysed further (glucose, fructose, ribose), oligosaccharides give 2–10 units (the disaccharides sucrose, maltose and lactose), and polysaccharides give many units (starch, cellulose, glycogen).

The key monosaccharide is glucose, an aldohexose ($\text{C}_6\text{H}_{12}\text{O}_6$ with an aldehyde group). It exists mostly as a six-membered cyclic pyranose ring, which creates a new stereocentre at C-1 (the anomeric carbon) giving two anomers, $\alpha$ and $\beta$; their interconversion in solution is called mutarotation. Fructose is a ketohexose (same formula but a keto group). Sugar units join through a glycosidic linkage (an ether bond between the anomeric carbon of one unit and a hydroxyl of another) — this is how di- and polysaccharides are built.

A distinction NEET tests often is reducing versus non-reducing sugars. A reducing sugar has a free anomeric (aldehyde/keto) group and so reduces Tollens' and Fehling's reagents — glucose, fructose, maltose and lactose are reducing. Sucrose (table sugar, glucose + fructose) is non-reducing because the glycosidic bond ties up the anomeric carbons of both units, leaving no free group. Sucrose's hydrolysis to glucose + fructose is called inversion (the optical rotation changes sign), giving 'invert sugar'.

The polysaccharides are all polymers of glucose but differ crucially in their links. Starch (the storage carbohydrate of plants) is made of $\alpha$-glucose units and has two parts — linear amylose and branched amylopectin; its $\alpha$-glycosidic links are digestible by humans. Cellulose (the structural material of plant cell walls) is made of $\beta$-glucose units in long straight chains; humans lack the enzyme for $\beta$-links, so we cannot digest cellulose (it is dietary fibre). Glycogen is 'animal starch', a highly branched glucose store in liver and muscle. The starch-vs-cellulose ($\alpha$ vs $\beta$) contrast is a guaranteed NEET point.

Figure — Carbohydrates: Classification and Structure
CarbohydrateKey fact
Glucosealdohexose; reducing; $\alpha/\beta$ anomers
Sucroseglucose+fructose; non-reducing
Starch$\alpha$-glucose; digestible (amylose+amylopectin)
Cellulose$\beta$-glucose; not digestible by humans
Worked Examples
1

Why is sucrose a non-reducing sugar while maltose is reducing?

Show solution

In sucrose the glycosidic bond joins the anomeric carbons of both glucose and fructose, so there is no free aldehyde/keto group to reduce Tollens'/Fehling's. Maltose has one free anomeric carbon, so it is reducing.

2

Both starch and cellulose are glucose polymers, yet humans digest only starch. Why?

Show solution

Starch has $\alpha$-glycosidic links, which human enzymes can hydrolyse. Cellulose has $\beta$-glycosidic links, and humans lack the enzyme to break them, so cellulose passes through as fibre.

✎ Self-Check — 5 questions0 / 5
Q1.

Glucose is classified as a/an:

Explanation: Six carbons with an aldehyde group: aldohexose.
Q2.

Which is a non-reducing sugar?

Explanation: Sucrose has no free anomeric group.
Q3.

The two anomers of glucose interconvert by:

Explanation: $\alpha \rightleftharpoons \beta$ is mutarotation.
Q4.

Cellulose is built from:

Explanation: $\beta$-glycosidic links — indigestible to humans.
Q5.

The storage polysaccharide in animals is:

Explanation: Glycogen = 'animal starch'.

NEET tip: reducing sugars (glucose, fructose, maltose, lactose) reduce Tollens'/Fehling's; sucrose does NOT. Starch = $\alpha$ (digestible); cellulose = $\beta$ (fibre); glycogen = animal store.

Proteins: Amino Acids, Structure and EnzymesTopic 2

Proteins are polymers of $\alpha$-amino acids — molecules that contain both an amino group ($-\text{NH}_2$) and a carboxyl group ($-\text{COOH}$) on the same ($\alpha$) carbon. About 20 standard amino acids build all proteins; those the body cannot make and must obtain from food are essential amino acids, the rest are non-essential. Because they carry both an acidic and a basic group, amino acids are amphoteric and usually exist as a zwitterion (an internal salt, $\text{H}_3\text{N}^+\text{–CHR–COO}^-$); the pH at which the zwitterion has no net charge is the isoelectric point.

Amino acids link through the peptide bond, an amide linkage ($-\text{CO}-\text{NH}-$) formed when the $-\text{COOH}$ of one acid condenses with the $-\text{NH}_2$ of the next, losing water. Two amino acids give a dipeptide, many give a polypeptide, and large polypeptides are proteins. The sequence of amino acids and the way the chain folds determine everything about a protein's function.

Protein structure is described at four levels. The primary structure is the exact sequence of amino acids. The secondary structure is local folding into an $\alpha$-helix or a $\beta$-pleated sheet, held together by hydrogen bonds. The tertiary structure is the overall three-dimensional shape of the whole chain (folded and held by various interactions). The quaternary structure is the assembly of two or more folded chains into one functional unit (haemoglobin, with four chains, is the classic example). NEET frequently asks which forces or features belong to which level.

When a protein is exposed to heat, strong acids or other stresses, it undergoes denaturation: its secondary and tertiary structures break down (the primary sequence remains), the molecule loses its specific shape, and it loses biological activity — boiling an egg or curdling milk are everyday examples. Finally, enzymes are specialised proteins that act as biological catalysts: they are highly specific, work under mild body conditions, and speed up reactions by lowering the activation energy (without being consumed). Vitamins and metal ions often help enzymes as coenzymes/cofactors — a link to the next module.

Figure — Proteins: Amino Acids, Structure and Enzymes
LevelWhat it is
Primaryamino-acid sequence (peptide bonds)
Secondary$\alpha$-helix / $\beta$-sheet (H-bonds)
Tertiaryoverall 3D fold of one chain
Quaternaryseveral chains assembled (e.g. haemoglobin)
Worked Examples
1

Why are amino acids said to exist as zwitterions?

Show solution

An amino acid has a basic $-\text{NH}_2$ and an acidic $-\text{COOH}$. The $-\text{COOH}$ donates its proton to the $-\text{NH}_2$ within the same molecule, giving an internal salt $\text{H}_3\text{N}^+\text{–CHR–COO}^-$ — the dipolar zwitterion.

2

What happens to a protein's structure when an egg is boiled?

Show solution

The protein is denatured: heat breaks the hydrogen bonds and other interactions that hold its secondary and tertiary structure, so it unfolds and aggregates (the white turns solid) and loses biological activity. The primary sequence is unchanged.

✎ Self-Check — 5 questions0 / 5
Q1.

The bond linking amino acids in a protein is the:

Explanation: Peptide (amide) bond, –CO–NH–.
Q2.

Amino acids exist mainly as:

Explanation: Internal salt (dipolar ion).
Q3.

The $\alpha$-helix and $\beta$-pleated sheet describe which level?

Explanation: Secondary structure, held by H-bonds.
Q4.

Denaturation of a protein destroys its:

Explanation: 2°/3° structure lost; primary sequence intact.
Q5.

Enzymes are biological catalysts made of:

Explanation: Enzymes are specialised proteins.

NEET tip: peptide bond = –CO–NH–. Primary (sequence) → secondary ($\alpha$-helix/$\beta$-sheet, H-bonds) → tertiary (3D) → quaternary (multi-chain). Denaturation loses 2°/3° (not primary). Enzymes = protein catalysts.

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Module 2

Nucleic Acids, Vitamins and Hormones

Nucleic Acids (DNA and RNA)Topic 3

Nucleic acids are the information molecules of the cell: DNA (deoxyribonucleic acid) stores and transmits genetic information, and RNA (ribonucleic acid) carries out protein synthesis. Both are long polymers (polynucleotides) built from repeating units called nucleotides.

Each nucleotide has three parts: a nitrogenous base, a pentose sugar, and a phosphate group. A base joined to the sugar alone (no phosphate) is a nucleoside; adding phosphate makes it a nucleotide — a distinction NEET likes to test. The nucleotides are linked through phosphodiester bonds between the phosphate of one and the sugar of the next, forming the sugar–phosphate backbone.

The bases are of two kinds: purines (double-ring) — adenine (A) and guanine (G); and pyrimidines (single-ring) — cytosine (C), plus thymine (T) in DNA and uracil (U) in RNA. The sugar is deoxyribose in DNA and ribose in RNA. So the three differences between DNA and RNA are: sugar (deoxyribose vs ribose), one base (thymine vs uracil), and strandedness (DNA is usually double-stranded, RNA usually single-stranded).

DNA's famous double helix (Watson and Crick) consists of two strands wound around each other and held by hydrogen bonds between complementary base pairs: A pairs with T (two hydrogen bonds) and G pairs with C (three hydrogen bonds). This base-pairing rule means the two strands carry the same information in complementary form, which is the basis of accurate replication. RNA comes in three working types — messenger (mRNA), transfer (tRNA) and ribosomal (rRNA) — that together translate the DNA message into proteins. The A–T (2 bonds) and G–C (3 bonds) pairing and the DNA-vs-RNA differences are perennial NEET questions.

Figure — Nucleic Acids (DNA and RNA)
FeatureDNARNA
Sugardeoxyriboseribose
BasesA, G, C, TA, G, C, U
Strandsdouble helixusually single
Base pairsA–T (2 H-bonds), G–C (3 H-bonds)
Worked Examples
1

What is the difference between a nucleoside and a nucleotide?

Show solution

A nucleoside is a base + sugar. A nucleotide is a base + sugar + phosphate — i.e. a nucleoside with a phosphate group added.

2

In DNA, which base pairs with guanine, and by how many hydrogen bonds?

Show solution

Guanine pairs with cytosine by three hydrogen bonds. (Adenine pairs with thymine by two.)

✎ Self-Check — 5 questions0 / 5
Q1.

A nucleotide consists of:

Explanation: Base + sugar + phosphate.
Q2.

The sugar present in RNA is:

Explanation: RNA has ribose; DNA has deoxyribose.
Q3.

Which base is found in RNA but not DNA?

Explanation: RNA uses uracil instead of thymine.
Q4.

In DNA, adenine pairs with thymine by:

Explanation: A–T = 2 hydrogen bonds.
Q5.

The purine bases are:

Explanation: Purines (double ring): adenine and guanine.

NEET tip: nucleoside = base+sugar; nucleotide = +phosphate. DNA: deoxyribose, A/G/C/T, double helix; RNA: ribose, A/G/C/U, single. A–T (2 H-bonds), G–C (3 H-bonds); purines A,G — pyrimidines C,T,U.

Vitamins and HormonesTopic 4

Vitamins are organic compounds that the body needs in small amounts for normal metabolism but mostly cannot synthesise, so they must come from the diet. They are grouped by solubility, which controls how they are stored and how often they are needed. Fat-soluble vitamins (A, D, E, K) dissolve in fats and are stored in the liver and fatty tissue, so they need not be eaten daily. Water-soluble vitamins (the B group and C) are not stored (excess is excreted in urine), so they must be supplied regularly.

Each vitamin has specific roles and a characteristic deficiency disease — a favourite NEET recall set. Vitamin A deficiency causes night blindness; vitamin B1 (thiamine) deficiency causes beriberi; vitamin C (ascorbic acid) deficiency causes scurvy (bleeding gums); vitamin D deficiency causes rickets in children and osteomalacia in adults; vitamin K deficiency impairs blood clotting; vitamin E is an antioxidant. Knowing the vitamin → disease pairs is essentially guaranteed marks.

Hormones are chemical messengers secreted directly into the blood by ductless (endocrine) glands; they travel to target organs and regulate processes such as growth, metabolism and reproduction. Chemically they are varied: some are steroids (the sex hormones testosterone and oestrogen, and cortisol), some are amino-acid derivatives (adrenaline, thyroxine), and some are proteins/peptides (insulin). Key examples are insulin (lowers blood glucose; its lack causes diabetes), adrenaline (the fight-or-flight hormone), and thyroxine (regulates metabolic rate; needs iodine, whose deficiency causes goitre).

It is important to distinguish the two. Vitamins are nutrients obtained from food and act mainly as coenzymes assisting enzymes, whereas hormones are made within the body by glands and act as regulatory signals. Both are needed in small quantities and both connect chemistry to physiology — the reason this applied topic appears in NEET. Together with carbohydrates, proteins and nucleic acids, vitamins and hormones complete the picture of the molecules that run living systems.

Figure — Vitamins and Hormones
Vitamin / hormoneRole / deficiency
Vitamin Avision; deficiency → night blindness
Vitamin Cdeficiency → scurvy
Vitamin Ddeficiency → rickets
Insulin / thyroxinelowers glucose / regulates metabolism (iodine)
Worked Examples
1

Name the deficiency diseases of vitamins C and D.

Show solution

Vitamin C deficiency causes scurvy (bleeding gums); vitamin D deficiency causes rickets in children (soft, deformed bones).

2

Give one key difference between a vitamin and a hormone.

Show solution

A vitamin is an organic nutrient obtained from the diet (the body cannot make it), while a hormone is a chemical messenger made within the body by an endocrine gland.

✎ Self-Check — 5 questions0 / 5
Q1.

The fat-soluble vitamins are:

Explanation: A, D, E, K are fat-soluble; B and C are water-soluble.
Q2.

Deficiency of vitamin C causes:

Explanation: Vitamin C deficiency → scurvy.
Q3.

The hormone that lowers blood glucose is:

Explanation: Insulin lowers blood glucose.
Q4.

Thyroxine, which regulates metabolic rate, requires the element:

Explanation: Thyroxine contains iodine; deficiency causes goitre.
Q5.

Which is true?

Explanation: Vitamins are dietary; hormones are body-made messengers.

NEET tip: fat-soluble = A,D,E,K (stored); water-soluble = B,C (daily). Learn vitamin→disease: A→night blindness, B1→beriberi, C→scurvy, D→rickets. Hormones = body-made messengers (insulin, adrenaline, thyroxine).

Quick Revision — Biomolecules

  • Carbohydrates are polyhydroxy aldehydes/ketones (or yield them on hydrolysis): mono- (glucose, fructose), oligo- (sucrose, maltose, lactose) and poly- (starch, cellulose, glycogen).
  • Reducing sugars have a free anomeric (–CHO/keto) group (glucose, maltose, lactose); sucrose is non-reducing (both anomeric carbons are linked).
  • Starch ($\alpha$-glycosidic, plant storage) is digestible; cellulose ($\beta$-glycosidic, structural) is not digestible by humans.
  • Proteins are polymers of $\alpha$-amino acids joined by peptide bonds (–CO–NH–). Structure: primary (sequence) $\rightarrow$ secondary ($\alpha$-helix, $\beta$-sheet) $\rightarrow$ tertiary $\rightarrow$ quaternary. Denaturation destroys 2°/3° structure.
  • Amino acids are amphoteric and exist as zwitterions; enzymes are protein biocatalysts.
  • Nucleic acids: nucleotide = base + sugar + phosphate. DNA pairs A–T (2 H-bonds) and G–C (3 H-bonds); DNA has deoxyribose + thymine, RNA has ribose + uracil.
  • Vitamins (fat-soluble A,D,E,K; water-soluble B,C) prevent deficiency diseases; hormones are chemical messengers from endocrine glands.

Frequently Asked Questions

What makes a sugar 'reducing', and why is sucrose non-reducing?
A reducing sugar has a free aldehyde or keto (anomeric) group that can reduce Tollens' or Fehling's reagent — glucose, maltose and lactose all qualify. In sucrose the anomeric carbons of both glucose and fructose are joined together in the glycosidic linkage, so neither free group remains, and sucrose does not reduce these reagents.
What is the difference between starch and cellulose?
Both are polymers of glucose, but starch is built from alpha-glucose units (alpha-glycosidic links), forming amylose and amylopectin that humans can digest and use for energy. Cellulose is built from beta-glucose units (beta-glycosidic links), giving long straight chains that act as plant structural material; humans lack the enzyme to break beta-links, so we cannot digest cellulose.
What are the four levels of protein structure?
Primary structure is the sequence of amino acids joined by peptide bonds. Secondary structure is local folding into alpha-helices or beta-pleated sheets held by hydrogen bonds. Tertiary structure is the overall three-dimensional folding of the whole chain. Quaternary structure is the assembly of two or more folded chains into one functional protein, like haemoglobin.
What is denaturation of a protein?
Denaturation is the loss of a protein's secondary and tertiary structure (its three-dimensional shape) when it is exposed to heat, acids, or other stresses, while the primary sequence stays intact. The protein loses its biological activity — a familiar example is the white of an egg turning solid and opaque when cooked.
How do DNA bases pair, and how does RNA differ from DNA?
In DNA, adenine pairs with thymine through two hydrogen bonds and guanine pairs with cytosine through three hydrogen bonds, holding the two strands of the double helix together. RNA differs in three ways: its sugar is ribose (not deoxyribose), it uses uracil in place of thymine, and it is usually single-stranded.

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