Cells rely on three primary classes of biological macromolecules:
Polysaccharides (≈ carbohydrates)
Proteins
Nucleic acids
Shared features
Each macromolecule is a polymer—a long chain of repeating building blocks (monomers).
Specific monomer → polymer mapping:
Monosaccharides (simple sugars) → polysaccharides
Amino acids → proteins
Nucleotides → nucleic acids
All polymer-building processes require energy and involve removal of water.
Polymerisation & Covalent Bond Formation
Adjacent monomers are connected by covalent bonds—strong bonds that demand an energy input to form.
Energy source: generally the hydrolysis of a high-energy phosphate bond in ATP (or a similar nucleotide).
ATP \rightarrow ADP + P_i + \text{energy}
Dehydration (condensation) reaction
Water (H2O) is expelled as the bond forms:
\text{Monomer}1 + \text{Monomer}2 \xrightarrow[\text{energy}]{\text{dehydration}} \text{Monomer}1{-}\text{Monomer}2 + H2O
Mechanism applies equally to sugars, amino acids, and nucleotides.
Hydrolysis – The Reverse Process
Hydrolysis reaction cleaves polymers back to monomers by adding water, essentially the exact opposite of dehydration:
\text{Polymer} + H2O \xrightarrow{\text{hydrolysis}} \text{Monomer}n
Practical cellular example: breaking stored glycogen into glucose → fuels ATP production.
Non-Covalent Interactions & 3-D Structure
Covalent backbones alone do not supply biological function; correct folding is essential.
In the aqueous cytoplasm, polymers spontaneously adopt specific 3-D conformations driven by non-covalent bonds:
Hydrogen bonds
Ionic (electrostatic) bonds
Properties of non-covalent bonds
Individually weak, form without external energy, and break easily.
In large numbers—dozens, hundreds, or thousands—they create substantial collective stability ("zipper" analogy).
DNA example
Two antiparallel nucleotide strands twist into a double helix.
Bases pair internally (non-covalent H-bonding) while the sugar–phosphate backbone remains solvent-exposed.
Cellular Functions of Macromolecules
Serve as sensors, transporters, regulators, binders, information warehouses, energy reservoirs, and structural components.
Effectiveness depends on precise 3-D conformation; misfolding generally inactivates function.
Carbohydrates (Polysaccharides)
Everyday term: carbohydrates—a major dietary category.
Core roles
Energy storage
Starch: plant storage polysaccharide (found in vegetables, grains).
Glycogen: animal storage polysaccharide (primarily in liver & muscle).
Both consist entirely of \alpha-glucose units.
Structural support
Cellulose: main structural component in plant cell walls.
Chitin: exoskeleton material in arthropods and cell walls of fungi.
Energy mobilization pathway
Glycogen \xrightarrow{\text{hydrolysis}} glucose \rightarrow ATP production.
Proteins
Diversity: thousands of distinct proteins, spanning catalytic, structural, transport, signaling, and regulatory roles.
Building blocks: 20 standard amino acids.
Formation
Amino acids linked by peptide bonds via dehydration → generate a polypeptide chain.
Folding & assembly
Polypeptide automatically folds into a unique conformation powered by hundreds of non-covalent (and occasional covalent, e.g., disulfide) interactions.
Some proteins function as single chains; others require oligomerisation (e.g., hemoglobin = 4 subunits).
Enzymatic Catalysis
Enzymes (nearly all proteins) accelerate reactions by lowering the activation energy barrier:
\text{Reactants} \xrightarrow[\small \text{low } E_a]{\text{enzyme}} \text{Products}
Activation energy analogy: a hill reactants must climb before descending to products; enzymes reduce hill height.
Additional Protein Functions (from transcript examples)
Structural: e.g., collagen (major component of connective tissues, skin, and bone). (Transcript cuts off mid-sentence, but collagen cited as example.)
Key Concept Map & Connections
Dehydration vs. hydrolysis forms a fundamental biochemical cycle: build polymers → store information/energy/structure → break polymers → release information/energy/subunits.
Energy economy centers on ATP hydrolysis coupling to covalent bond formation.
Proper function hinges on hierarchical bonding:
Covalent backbone confers permanence.
Non-covalent network directs folding, specificity, and dynamic interactions.
Real-world relevance
Dietary choices (carbohydrate intake) directly influence glycogen stores and metabolic ATP generation.
Protein folding diseases (e.g., misfolded enzymes) illustrate critical dependence on non-covalent integrity.
Industrial enzymes harness activation-energy reduction to drive bio-manufacturing.