Part 3 · Chapter 30

Biomolecules

The chemistry of life — sugars for energy, proteins for structure and catalysis, vitamins for regulation, and the nucleic acids that carry the code

Fundamentals of Chemistry Prof. Mithun Mondal Reading time ≈ 55 min
i What you'll learn
  • How carbohydrates are classified, and the difference between reducing and non-reducing sugars.
  • The open-chain and cyclic structure of glucose and its key reactions.
  • Amino acids, the zwitterion, the peptide bond, and the four levels of protein structure.
  • What enzymes are and why they are such efficient, specific catalysts.
  • The fat- and water-soluble vitamins and their deficiency diseases.
  • The structure of nucleic acids — nucleotides, the double helix and base pairing.
Section 30-1

What Are Biomolecules?

Biomolecules are the organic compounds that build and run living cells. Four great families dominate: carbohydrates (energy and structure), proteins (structure and catalysis), nucleic acids (information), and smaller regulators such as vitamins and hormones. All are built from the functional groups met earlier in Part 3 — they are organic chemistry doing the work of life.

Section 30-2

Carbohydrates: Classification

Carbohydrates are polyhydroxy aldehydes or ketones, or compounds that give these on hydrolysis. They are classified by how many sugar units they yield.

ClassHydrolysisExamples
Monosaccharidecannot be hydrolysedglucose, fructose, ribose
Disaccharidegives 2 monosaccharidessucrose, maltose, lactose
Polysaccharidegives many unitsstarch, cellulose, glycogen
Reducing vs non-reducing. A reducing sugar has a free aldehyde or ketone group, so it reduces Tollens' and Fehling's reagents — glucose, fructose, maltose and lactose all do. Sucrose is the exception: its two anomeric carbons are locked together in the glycosidic bond, leaving no free carbonyl, so it is non-reducing.
Section 30-3

Glucose: Structure & Reactions

Glucose (\(\ce{C6H12O6}\)) is an aldohexose — a six-carbon sugar with an aldehyde group. It exists in an open-chain form and, predominantly, as a cyclic six-membered (pyranose) ring with two anomers, \(\alpha\) and \(\beta\), which interconvert in solution (mutarotation).

CHO (CHOH)₄ CH₂OH open chain O pyranose ring (α / β)
Glucose — open-chain aldehyde ⇌ cyclic pyranose
ReagentProductReveals
\(\ce{HI}\), heat\(n\)-hexanestraight C₆ chain
\(\ce{Br2}\) watergluconic acid\(\ce{-CHO}\) group (oxidised)
conc. \(\ce{HNO3}\)saccharic acid\(\ce{-CHO}\) and \(\ce{-CH2OH}\) (both ends)
\(\ce{NH2OH}\)oxime\(\ce{-CHO}\) group
acetic anhydridepentaacetatefive \(\ce{-OH}\) groups
Section 30-4

Di- & Polysaccharides

Sugar units join through a glycosidic linkage (an ether-like C–O–C bond). The same glucose monomer, linked differently, builds molecules with utterly different roles.

CarbohydrateBuilt fromRole
Sucroseglucose + fructosetransport sugar (non-reducing)
Maltoseglucose + glucosereducing disaccharide
Lactoseglucose + galactosemilk sugar (reducing)
Starchα-glucose (amylose + amylopectin)energy store in plants
Celluloseβ-glucosestructural fibre in plants
Glycogenα-glucose (branched)energy store in animals
One monomer, two destinies. Starch (\(\alpha\)-1,4 links) is digestible and stores energy; cellulose (\(\beta\)-1,4 links) is rigid and indigestible to humans. The only difference is the geometry at the linking carbon — proof that in biomolecules, shape is function.
Section 30-5

Amino Acids & the Zwitterion

Proteins are built from α-amino acids — molecules with both an amino (\(\ce{-NH2}\)) and a carboxyl (\(\ce{-COOH}\)) group on the same carbon. Twenty standard amino acids occur; those the body cannot make are essential. Because each carries an acid and a base, an amino acid exists largely as a dipolar zwitterion.

H₂N–CHR–COOH ⁺H₃N–CHR–COO⁻ internal proton transfer → dipolar zwitterion (amphoteric)
The zwitterion — an internal acid–base salt
⚖️
Zwitterion & isoelectric point
amphoteric · net charge zero at the isoelectric point (pI)

Being both acid and base, an amino acid reacts with either, and at a specific pH — its isoelectric point — it carries no net charge and is least soluble. Amino acids join through the peptide bond (\(\ce{-CO-NH-}\)), an amide link, to build proteins.

Section 30-6

Proteins & Their Structure

A protein is a polymer of amino acids folded into a precise shape. Chemists describe that shape at four levels, each held together by different forces.

LevelWhat it isHeld by
Primarysequence of amino acidspeptide (covalent) bonds
Secondaryα-helix, β-pleated sheethydrogen bonds
Tertiaryoverall 3-D foldvarious side-chain interactions
Quaternaryassembly of subunitssame interactions between chains
Denaturation. Heat, acid or heavy metals can unravel a protein's secondary, tertiary and quaternary structure while leaving the primary sequence intact — the coagulation of egg white on cooking is exactly this. The chain is still whole, but its biological shape, and hence its function, is lost.
Section 30-7

Enzymes

Enzymes are proteins that act as biological catalysts. Like all catalysts they speed reactions by lowering the activation energy, but they do so with extraordinary specificity and efficiency — a single enzyme often acts on just one substrate, fitting it like a lock and key. Most enzymes are named after their substrate with the suffix -ase (maltase, urease).

The link back to catalysis. Everything you learned about catalysts in surface chemistry applies here: enzymes provide an alternative low-energy pathway. What sets them apart is the geometrically matched active site, which gives precision no metal surface can match.
Section 30-8

Vitamins

Vitamins are organic compounds needed in tiny amounts to keep metabolism running; the body cannot make most of them. They split into fat-soluble (A, D, E, K) and water-soluble (B-complex, C). A shortage causes a characteristic deficiency disease.

VitaminSolubilityDeficiency disease
Afatnight blindness, xerophthalmia
\(\ce{B1}\) (thiamine)waterberi-beri
C (ascorbic acid)waterscurvy
Dfatrickets, osteomalacia
Kfatpoor blood clotting
Why solubility matters. Water-soluble vitamins are excreted readily and must be eaten regularly; fat-soluble ones are stored in body fat and can build up to harmful levels if grossly over-supplied. Solubility quietly shapes both deficiency and toxicity.
Section 30-9

Nucleic Acids

Nucleic acids — DNA and RNA — store and transmit genetic information. They are polymers of nucleotides, each a unit of a nitrogenous base, a pentose sugar, and a phosphate. (A base plus sugar alone is a nucleoside.)

A = T G ≡ C (H-bonded pairs) antiparallel double helix
The DNA double helix — complementary base pairing
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DNA vs RNA
DNA: deoxyribose, bases A-T-G-C, double helix · RNA: ribose, A-U-G-C, single strand

In DNA the bases pair specifically — adenine with thymine, guanine with cytosine — held by hydrogen bonds, giving the two strands their complementary double helix. DNA stores the genetic code and is copied during replication; RNA (mRNA, tRNA, rRNA) carries that code into protein synthesis.

Worked Examples

Putting It to Work

1 Reducing or not?

Problem. Classify glucose, maltose and sucrose as reducing or non-reducing sugars.

Solution. A free carbonyl makes a sugar reducing; sucrose has none:

Working
\[ \text{glucose, maltose → reducing};\quad \text{sucrose → non-reducing} \]
2 A glucose reaction

Problem. What does the reaction of glucose with \(\ce{HI}\) prove about its structure?

Solution. It gives \(n\)-hexane:

Working
\[ \ce{glucose ->[HI] }\textit{n}\text{-hexane} \Rightarrow \text{six carbons in a straight chain} \]
3 The zwitterion

Problem. Why is an amino acid amphoteric, and what is its isoelectric point?

Solution. It bears both \(\ce{-COO-}\) and \(\ce{-NH3+}\):

Working
\[ \text{reacts with acid \& base};\ \text{pI} = \text{pH of zero net charge} \]
4 Denaturation

Problem. When egg white is boiled it sets solid. Which protein structures are lost, and which survives?

Solution. Heat disrupts the higher-order folding only:

Working
\[ \text{2°, 3°, 4° lost};\quad \text{1° (sequence) intact} \]
5 Base pairing

Problem. A DNA strand has 30% adenine. What percentage of cytosine does the molecule contain?

Solution. A = T = 30%, so G + C = 40%, split equally:

Working
\[ \%\ce{C} = \tfrac{40}{2} = \textbf{20\%} \]
6 Vitamin deficiency

Problem. Name the disease caused by lack of vitamin C and its solubility class.

Solution. Vitamin C is water-soluble:

Working
\[ \textbf{scurvy};\quad \text{water-soluble vitamin} \]
Review

Chapter Summary

Carbohydrates

Mono/di/polysaccharides; reducing sugars (free carbonyl) vs non-reducing sucrose.

Glucose

Aldohexose; open-chain ⇌ pyranose; reactions reveal \(\ce{-CHO}\), 5 \(\ce{-OH}\), C₆ chain.

Amino acids

Amphoteric zwitterions; isoelectric point; peptide bond joins them.

Proteins

Four structural levels; denaturation loses shape but not sequence.

Vitamins

Fat-soluble (A,D,E,K) vs water-soluble (B,C); each deficiency has a disease.

Nucleic acids

Nucleotides; DNA double helix; A-T, G-C pairing; DNA stores, RNA translates.

Practice

Problems

For each item, first decide which family it concerns — carbohydrate, protein, vitamin or nucleic acid — then apply the relevant structure–function idea. Difficulty rises down the list.

  1. Define a carbohydrate and classify mono-, di- and polysaccharides with examples.
  2. What makes a sugar reducing? Why is sucrose non-reducing?
  3. List three reactions of glucose and state what each reveals about its structure.
  4. Compare starch and cellulose in terms of linkage and biological role.
  5. Explain why an amino acid exists as a zwitterion and define the isoelectric point.
  6. What is a peptide bond? Name the four levels of protein structure.
  7. Describe denaturation and say which structural level survives it.
  8. Why are enzymes described as highly specific catalysts?
  9. Classify vitamins by solubility and match A, C and D to their deficiency diseases.
  10. Describe the components of a nucleotide and distinguish it from a nucleoside.
  11. State the base-pairing rules in DNA and the forces that hold the pairs.
  12. Give three differences between DNA and RNA.
Tip: read every biomolecule as structure dictating function. A free carbonyl makes a sugar reducing; an α-1,4 vs β-1,4 link decides digestible starch from rigid cellulose; a protein's fold makes it work and denaturation breaks it; complementary base shapes let DNA copy itself faithfully. Ask "what does the structure let this molecule do?" and the biology follows from the chemistry.