Water and Essential Ions

Water isn't just for staying hydrated - it's literally where life happens. Most of your cellular reactions take place in aqueous solutions, making water the ultimate biological workspace. It also acts as a transport highway, carrying nutrients and waste products throughout living organisms.

Here's what makes water special: hydrophilic molecules (like sugars) love water and dissolve easily, while hydrophobic molecules (like fats) avoid it completely. This creates the perfect conditions for cell membranes and other biological structures to form.

Your body relies on buffers to maintain the right pH levels because even tiny changes can completely mess up protein function. Think of buffers as biological bouncers - they keep everything stable so your enzymes can work at their optimum pH.

Key Point: Essential ions like calcium (Ca²⁺) strengthen bones and help muscles contract, iron (Fe²⁺) carries oxygen in haemoglobin, and magnesium (Mg²⁺) makes photosynthesis possible in plants.

Introduction to Carbohydrates

Carbohydrates are your body's favourite fuel source, made from just carbon, hydrogen and oxygen in a 2:1 hydrogen to oxygen ratio. These organic molecules start as simple monomers that link together through polymerisation to create complex structures.

Glucose is the star of the show - a hexose monosaccharide with the formula C₆H₁₂O₆. It comes in two forms: α-glucose and β-glucose, which are isomers (same molecular formula, different arrangement). This tiny structural difference completely changes how they behave in your body.

Fructose is another important monosaccharide you'll encounter, especially in fruits. While it has the same formula as glucose, its different structure gives it unique properties.

Remember: Understanding the difference between α-glucose and β-glucose is crucial - it determines whether carbohydrates become energy storage (starch) or structural support (cellulose).

Disaccharides and Polysaccharides

When two monosaccharides get together, they form disaccharides through condensation reactions, creating glycosidic bonds. This process is reversible - hydrolysis reactions can break them apart again when your body needs the individual sugars.

Maltose $two α-glucose molecules$ forms when starch breaks down during digestion. Sucrose $α-glucose + fructose$ is how plants transport carbohydrates through their phloem - think of it as plant blood sugar.

Polysaccharides are the heavy-duty carbohydrates with the formula (C₆H₁₀O₅)ₙ. Starch comes in two forms: amylose has straight chains that coil into spirals, while amylopectin has branched chains thanks to both α-1,4 and α-1,6 glycosidic bonds.

Study Tip: Remember that condensation reactions build larger molecules by removing water, while hydrolysis reactions break them down by adding water back.

Storage Carbohydrates

Starch is nature's perfect storage solution because it ticks every box for efficiency. Amylose and amylopectin pack loads of glucose into tiny spaces, and because they're insoluble, they won't mess with your cell's water potential. Being large molecules means they stay put and won't leak through cell membranes.

The branching in amylopectin creates loads of terminal ends that can be quickly hydrolysed when your body needs energy fast during high respiratory demand. It's like having multiple access points to your energy stores.

Glycogen is the animal and fungal version of starch, stored as small granules mainly in your liver and muscle cells. It's similar to amylopectin but even more branched with shorter chains, making it the ultimate quick-access energy store.

Real-world connection: When you exercise, your muscles rapidly break down glycogen to release glucose for energy - those extra branches mean faster fuel delivery!

Structural Carbohydrates and Introduction to Lipids

Cellulose gives plants their strength using β-glucose monomers with alternate molecules rotated 180°. This rotation allows hydrogen bonds to form cross-linkages between adjacent chains, creating incredibly strong microfibrils that make up plant cell walls.

The lattice structure of cellulose microfibrils arranged in multiple planes gives plants amazing tensile strength - that's why wood is so strong and flexible.

Lipids are completely different beasts - they're large macromolecules but not polymers. They're hydrophobic $water-hating$ but dissolve in organic solvents like alcohol. Made from carbon, hydrogen and oxygen, they include triglycerides, phospholipids, waxes and steroids.

Triglycerides consist of glycerol plus three fatty acids joined by ester bonds through condensation reactions. Each fatty acid has a long hydrocarbon tail with a carboxyl group $-COOH$ at one end.

Fun fact: Cellulose is the most abundant organic polymer on Earth, yet humans can't digest it because we lack the enzymes to break β-1,4 glycosidic bonds!

Types of Lipids

Saturated fatty acids have only single C-C bonds, while unsaturated fatty acids contain at least one C=C double bond. Monounsaturated means one double bond; polyunsaturated means multiple double bonds. These differences affect how lipids behave - unsaturated fats are usually liquid at room temperature.

Triglycerides make excellent energy stores and provide crucial insulation and protection. They pack more than twice the energy per gram compared to carbohydrates, making them your body's long-term fuel reserves.

Phospholipids are like triglycerides with a twist - one fatty acid is replaced by a phosphate group. This creates polar molecules with hydrophilic heads (love water) and hydrophobic tails (hate water), perfect for forming cell membranes.

Cholesterol is a steroid that sits among the phospholipid chains in membranes, helping to maintain membrane fluidity and stability.

Memory tip: Think of phospholipids as having personalities - heads that love water and tails that run away from it, creating the perfect biological barrier!

Protein Structure and Function

Proteins are the workhorses of your cells, containing carbon, hydrogen, oxygen, nitrogen and usually sulphur. These large polymers are built from amino acid subunits, and their function is directly linked to their shape.

All amino acids share the same basic structure but differ in their R groups, which determine their properties. Peptide bonds form through condensation reactions - two amino acids make a dipeptide, many create a polypeptide.

Primary structure is simply the sequence of amino acids. Secondary structure includes α-helixes (coiled chains) and β-pleated sheets (folded parallel chains), both held by hydrogen bonds. Tertiary structure creates complex 3D shapes through further folding, forming globular proteins where shape is crucial for function.

Heat can break the hydrogen and disulphide bonds that maintain protein shape, causing denaturation - think of cooking an egg white!

Key insight: A protein's amino acid sequence determines everything else - change one amino acid and you might completely alter the protein's function!

Advanced Protein Structures

Quaternary structure occurs when multiple polypeptide chains combine to create functional proteins. Conjugated proteins team up with non-protein prosthetic groups - like the haem group in haemoglobin that carries oxygen.

Fibrous proteins like collagen have structural roles and are incredibly strong and stable. Collagen uses three identical polypeptides wound together and held by hydrogen bonds, creating the tough material found in tendons that connects muscle to bone.

Globular proteins are round and functional (like enzymes), while fibrous proteins are long and structural. Globular proteins are more sensitive to temperature and pH changes but are generally water-soluble, unlike their fibrous counterparts.

Prions are misfolded proteins that can replicate and cause diseases like BSE ('mad cow disease') and vCJD in humans. They have incredibly long incubation periods of 5-10 years and can be inherited through mutations.

Clinical connection: Understanding protein structure helps explain diseases - from sickle cell anaemia (altered haemoglobin) to prion diseases that devastate brain tissue.

Nucleic Acids Fundamentals

Nucleic acids are your genetic blueprint, built from nucleotides that each contain three components: a pentose sugar, phosphate group, and nitrogenous base. These link together through phosphodiester bonds formed in condensation reactions.

DNA (deoxyribonucleic acid) uses the sugar deoxyribose and includes the base thymine. RNA (ribonucleic acid) uses ribose sugar and uracil instead of thymine. This seemingly small difference creates molecules with completely different roles.

DNA forms a double helix with two anti-parallel strands held by hydrogen bonds between complementary base pairs: adenine with thymine and guanine with cytosine. The helix makes one complete turn every 10 base pairs.

RNA is single-stranded and shorter than DNA, coming in three main types: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA).

Amazing fact: If you stretched out all the DNA in one human cell, it would reach about 2 metres long, yet it fits into a nucleus smaller than a pinhead!

DNA and RNA Functions

DNA contains the primary genetic code that determines amino acid sequences in proteins. Every gene is a section of DNA coding for a specific polypeptide, making DNA the master controller of protein synthesis.

The sequence of DNA bases directly determines the amino acid sequence of polypeptides through the genetic code. This code is nearly universal across all living organisms, showing our shared evolutionary heritage.

mRNA acts as a messenger, carrying the genetic code from DNA in the nucleus to ribosomes in the cytoplasm where proteins are made. tRNA delivers specific amino acids to the mRNA during protein synthesis, while rRNA forms over half the mass of each ribosome.

This system allows your cells to produce thousands of different proteins from the same DNA blueprint, controlling everything from enzyme production to hormone synthesis.

Big picture: DNA stores the information, RNA reads and implements it - together they control every aspect of what makes you uniquely you!