1. Proteins: primary structure and biological functions. Protein classes and their functions. Structure and properties of amino acids. 2. Three-dimensional structure of proteins. Entropy, solvation, energetic principles. Secondary, tertiary and quaternary structure. 3. Protein folding: factors that determine it. Fibrous proteins. Globular proteins. Molecular chaperones. 4. Structure determination. Introduction to protein purification and characterisation techniques. Crystallography, X-ray diffraction. NMR. Electron microscopy. Cryo-microscopy. Structure refinement, modelling. predictive modelling. 5. Introduction to conformational diseases. 6. Relationship between structure and function in proteins: oxygen transport proteins. Myoglobin and haemoglobin. Allosterism, cooperativity and regulation. Molecular pathology. Structural proteins. 7. Biological catalysts, enzyme kinetics and regulation. Cofactors. 8. Inhibitors. Catalytic strategies. Regulation of enzyme activity. Classification and nomenclature of enzymes. 9. Protein degradation. Ubiquitin/Proteasome. 10. DNA structure. Base recognition. A, B and Z forms. Nucleosomes, heterochromatin. Histones. 11. Replication. Polymerases, helicases and topoisomerases. Origins of replication in eukaryotes and prokaryotes. 12. Transcription factors. Structure of promoter and terminator regions. RNA polymerases. 13. Recombination. Recombination complexes. 14. Translation machinery. mRNA, tRNA, rRNA aminoacyl synthetases, ribosomes.

Classroom lectures. Face-to-face classes: reduced (workshops, seminars, case studies). Student individual work. Final exam. Seminars and lectures supported by computer and audiovisual aids. Practical learning based on cases and problems, and exercise resolution. Individual and group or cooperative work with the option of oral or written presentation. Individual and group tutorials to resolve doubts and queries about the subject.