K16: Knows the structural mechanisms and systems involved in the immune response, and the functioning and development of the nervous system. S1: Uses a variety of techniques to find, manage, integrate and critically evaluate available information for the development of professional activities in Neuroscience, especially in the digital sphere S5: Appropriately uses the scientific and technical vocabulary of the different subfields within Neuroscience. C1: Apply knowledge about the biological basis of Central Nervous System (CNS) disorders and their effects to the development of improved diagnostics and treatments. C2: Apply knowledge about the organisation, structure and function of the Central Nervous System (CNS) to contribute to the evolution and improvement of technologies and systems for computing, data handling and analysis. C5: Apply your neuroscience knowledge in a unifying and integrated fashion as part of a multidisciplinary team (pharmaceutical sector, health industry, diagnostic techniques, health information technologies, government agencies and regulatory bodies. C7: Apply the scientific and technical principles you acquired during your undergraduate training, together with your own natural learning capabilities, to better adapt to novel opportunities arising from scientific and technological development.

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.