lipids and proteins

C , H , O , N

• detects presence of protein • blue to lilac

• detects presence of lipids • add ethanol and shake • add water • milky, white emulsion

• amine group (NH2) • carboxylic group (COOH) • R group (20 variations)

sequence of a chain of amino acids

hydrogen bonds cause folding into alpha helices or beta pleated sheets

further folding into 3D structure due to ionic bonds, hydrogen bonds, disulphide bridges and hydrophobic interactions

made of more than one polypeptide chain

• long strands of polypeptide chain and little to no tertiary structure • structural properties • insoluble • keratin, collagen

• polypeptide is folded and has 3D structure as result of internal bonding • enzymes, transport, antibodies • soluble • unstable structure

• made of 4 polypeptide chains • contains prosthetic group (non-protein group)

variable group that determines the properties of the amino acid

• via condensation reactions • forms peptide bonds between amino acids

C , H , O - more hydrogen than carbs

• 3 fatty acids • 1 glycerol • 3 ester bonds, via cooh of fatty acid and oh of glycerol • hydrophobic

not made up of monomers

• high ratio of energy storing carbon - hydrogen bonds • high ratio of hydrogen to oxygen atoms = metabolic water source • insoluble in water

saturated = contains only single bonds between carbon atoms unsaturated = contains double bonds between carbon atoms

• glycerol molecule • phosphate group replaces one fatty acid • 2 fatty acids

• hydrophilic phosphate heads exposed to water • hydrophobic fatty acid tails position away from water

different sequences of amino acids causing different types/ numbers of bonds (ionic,hydrogen and disulphide) folding of protein is different