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Biomolecule activity Key: Coke bottle lollies (and one bag of red frogs) = glucose/ribose Mixed lollies (gummy bears, pineapple, milk bottle = amino acids Lips, strawberry, raspberry, funky twirly lollie = bases/DNA Banana, 3 worms, teeth = Fats/lipids Banana = glycerol, worms = fatty acids, Teeth/red frog (use the teeth for the phospholipid and the frog for the DNA) = phospho 1 coke bottle/red frog (ribose) = DNA Background 1. Carbohydrates Starch – stored energy (glucose) in plants (insoluble), polysaccharide. Glucose units orientated in the same direction. Alpha glucose Glucose, fructose, galactose, ribose – monosaccharides Glycogen – storage of glucose in animals in the liver Cellulose – polysaccharide (3000 or more glucose units) Sucrose, lactose, maltose – disaccharide Condensation reaction – when two monosaccharides bond together (water is formed and therefore lost) Basis for the synthesis of carbohydrates, proteins, lipids, nucleic acid Monosaccharide, disaccharide, polysaccharide Hydrolysis – cleavage of chemical bonds with the addition of water. Saccharification Sucrose can be hydrolysed, forming two monosaccharides – glucose and fructose 2. Protein – composed of polymers (long chains of repeating units)of amino acids joined together by peptide bonds – contains nitrogen. Other components – carbon, hydrogen, oxygen, sulphur and sometimes phosphorous. Typical – 400 amino acids The sequence of amino acids in the chain determine how the chain will fold up to make protein. So different proteins have different 3 dimensional shapes. 3D shape determines its function. Shape determines what it can interact with – like a lock and key Functions – Structural – spindal fibres – mitosis, hair, nails Enzymes – catalyse biological reactions Hormones Antibodies Primary protein structure – linear sequence of a chain of amino acids Secondary protein structure- folding of the peptide chain e.g. double stranded DNA Tertiary protein structure – the 3D structure of a protein or nucleic acid. This is determined by a variety of bonding interactions between side chains which may cause folding, bending and loops in the protein chain. Disulphide bonds Hydrogen Bonds Quaternary protein structure – protein consisting of more than one amino acid chain Arrangement of multiple protein subunits. Polypeptide- 10 – 100amino acids Types of bonds Peptide bonds – carboxyl group (R-COOH) of one amino acid to the amino group of another amino acid –CH3-NH2 R = long chain of hydrocarbons 3. DNA Ribose C5H10O5 monosaccharide –RNA- alternates with phosphate to form backbone of RNA group Deoxyribose C5H10O4– DNA- replacement of hydroxyl group (OH) by hydrogen (H) Bond between bases – hydrogen bond = high tensile strength Adenine and guanine are purine bases found in both DNA and RNA Cytosine is a pyrimidine base found in both DNA and RNA Thymine and Uracil are pyrimidine bases found only in DNA or RNA Nucleotides = monomers 4. Fats Lipids – oils/fats – hydrolysed by the enzyme lipase to give fatty acid and glycerol Glycerol C3H8O3 – structural component of lipids, phospholipids and triglycerides Fatty acids – carboxylic group COOH and aliphatic tail (R) R- COOH Insoluble in water High energy content Storage Other uses Triglyceride – lipid molecule made up of one unit of glycerol and 3 fatty acids
