Structural and ionic properties of amino acids. Peptides, the peptide bond, primary, secondary, tertiary and quaternary structure of proteins. Interactions that stabilise protein structure, denaturation and renaturation of proteins. Introduction to methods for the purification of proteins, amino acid composition, and sequence determinations. Introduction to enzyme kinetics and enzyme inhibition. Allosteric enzymes, regulation of enzyme activity, active centres and mechanisms of enzyme catalysis. Examples of industrial applications of enzymes. Practical training in laboratory techniques and Good Laboratory Practice. Techniques for the quantitative and qualitative analysis of biological molecules. Processing and presentation of scientific data.