Structure, function, bioinformatics and biochemical analyses of nucleotides, oligonucleotides, amino acids, proteins and ligands and their organisation into hierarchial, higher order structures and interdependent systems. Principles of structure-function relationships. Protein folding, sequence motifs and domains, higher order and supramolecular structure, self-assembly, conjugated proteins, post-translational modifications. Principles of molecular recognition in protein-ligand, protein-protein, protein-DNA, protein-RNA, DNA-DNA, DNA-ligand, DNA-RNA and RNA-RNA interactions. The RNA structural world, RNAi, miRNA and ribosomes. Cellular functions of coding and non-coding nucleic acids. Population-specific mutations in disease. Global analysis of proteins through proteomics. Basic principles of nuclear magnetic resonance spectroscopy, mass spectrometry and X-ray crystallography. Protein purification and characterization including, pI, molecular mass, amino acid composition and sequence. Mechanistic aspects and regulation of information flow from DNA via RNA to proteins and back. Lectures incorporate the latest insights into the central dogma of biochemistry and viral polymerases which reverse the information flow ensuring students are prepared for a competitive job market. Practical training include hands-on practical sessions for nucleic acid purification, sequencing and structure characterisation, protein production purification (including SDS-PAGE) and sequence analysis including mass spectrometry, protein structure analysis by 3D protein modelling and protein folding (Bioinformatics).