A molecule is polar when it has an unequal distribution of charge. This unequal distribution creates full or partial negative and positive charges.
Hydrophilic
Polar molecules are hydrophilic, attract water (water loving)
Hydrophobic
Non-polar molecules are hydrophobic, repel water (water hating)
Monomers
May also have distinct functions: Energy source, energy carrier (building blocks)
Components of carbohydrates
Carbon
Hydrogen
Oxygen (water)
Monosaccharides
Simple sugars, the building blocks of carbohydrates
Molecular formula of carbohydrates
n x CH2O, where n = 3, 4, 5 or 6
Functional groups of carbohydrates
Carbonyl and Hydroxyl
Properties of carbohydrates
Hydrophilic, polar, water soluble
Aldoses and ketoses
Monosaccharides are classed as aldoses or ketoses depending on whether they contain an aldehyde or a ketone group
Ring formation of monosaccharides
In aqueous solution, 5 and 6 carbon sugars spontaneously form ring structures, the carbonyl (aldehyde or keto) group reacts with a hydroxyl group
Optical isomers
Monosaccharides can occur as optical isomers or enantiomers (D- or L- isomers) - mirror image forms
Most naturally occurring sugars are D- isomers
α- and β- forms of glucose
When glucose is in the ring structure, the hydroxyl attached to carbon 1 (aldehyde) has two possible positions (α- and β-), which interconvert rapidly in solution
Complex carbohydrate formation
Formed by glycosidic bond between monosaccharides. The α- or β- configuration is 'locked' when the bond is formed.
Disaccharides
Two monosaccharides linked by a glycosidic bond
Polysaccharides
Polymers of glucose acting as energy stores (starch- plants (amylose and amylopectin), glycogen- animals)
Structure of glycogen
Glycogen has a similar chemical structure to amylopectin, but with more branches. Chains- α-1,4 glycosidic bonds, Branches- α-1.6 glycosidic bonds
Sugars can be modifying and linked to lipids or proteins. Complex oligosaccharides (a few saccharides) can form recognition molecules on cell surfaces e.g., blood group determinants.
Lipids
Molecules in cells that are water-insoluble (hydrophobic) but soluble in organic solvents, including triacylglycerols, glycerophospholipids, steroids and cholesterol
Fatty acids
The monomeric building blocks of triacylglycerols and glycerophospholipids. The length and structural formula (saturated/ unsaturated) of the fatty acid carbon chain determines its physical properties (shape, melting point- longer + saturated = higher melting point)
Triacylglycerols
Formed by ester linkages between fatty acids and glycerol. Important energy storage molecules, hydrophobic (insoluble) so stored as fat droplets within cells.
Glycerophospholipids
Also based on glycerol, but one fatty acid is replaced by a phosphate group. The phosphate group is also linked to a hydrophilic 'head group.' They are amphipathic (hydrophilic head and hydrophobic tails) and form the cell membrane.
Steroids and Cholesterol
The steroid template (fused alkyl rings) is the basis for steroid hormones and the sterol lipid, cholesterol.
Functions of cholesterol
Necessary component of animal cell membrane, rigid structure inserts between glycerophospholipids – modulates membrane fluidity at both ends of the temperature scale
Nucleic acids
Ribonucleic acid and deoxyribonucleic acid (RNA / DNA), act as information molecules for the cell
Nucleotides
Building blocks of RNA and DNA, consisting of a pentose sugar, nitrogenous base, and phosphate
Pentose sugars
Ribose in RNA and Deoxyribose in DNA
Nitrogenous bases
A, C, G, T found in DNA
A, C, G, U found in RNA
Formation of nucleic acids
Nucleotides join together to form nucleic acids, joined by phosphodiester bonds. The base-pair sequence of DNA forms the genetic code.
Nucleotides also have other functions: ATP, which carries chemical energy in its phosphoanhydride bonds
Proteins
Carry out the mechanical, structural and transport functions of the body, and play a crucial role as enzymes (biological catalysts). Different proteins display a wide variety of shapes and sizes, determined by the information in the DNA sequence of the gene.
Protein folding
Proteins fold up spontaneously from linear chains of amino acids
Amino acids
Building blocks of proteins, 20 amino acids, water soluble and electrically charged at physiological pH, each differing in the properties of its side group (R group)
Peptide bond formation
In polypeptides, amino acids are linked by peptide bonds. Side chains (R groups) are not involving in peptide bonding. Interactions of side chains determine how proteins fold
pH is the measure of free hydrogen ions (H+) in a solution, ranging from 0-14 and determining a solution's acidity or alkalinity. The higher the H+, the lower the pH (more acidic).
Acid
A H+ ion (proton) donor
Base
A H+ ion (proton) acceptor
Strong acids and bases
Strong acids completely dissociate in a solution, strong bases readily accept H+ from an acid
Weak acids and bases
Weak acids only dissociate partially and are a poor source of hydrogen ions, weak bases are poor H+ acceptors and only partially dissociate