The students will understand how the atomic structure of biological molecules is discovered and how this knowledge is applied in modern drug discovery. If interested in this subject - they may continue their careers in the drug development industry.
- Principles of protein structure.
- Classification of protein folds.
- Anatomy and taxonomy of nucleic acids and macromolecular complexes.
- Overview of experimental methods of structural biology: cryo-EM.
- Principles of macromolecular crystallography.
- Protein handling and crystallization.
- Phasing methods in macromolecular crystallography.
- Electron density maps and model building.
- Protein Data Bank (PDB) and model validation.
- Examples of structure-based drug design.
- Protein handling and crystallization including robotic crystallization.
- Protein crystal handling, cryoprotection and X-ray diffraction experiments.
- Electron density maps and their interpretation.
- PDB and bioinformatics tools for protein analysis.
- An exercise in structure-guided drug design.
- Protein model building.
- 5 meetings with student seminars presenting assignments from current literature with discussion.
The course will teach the students:
- how the atomic 3D structure of biological macromolecules, proteins, nucleic acids and their complexes, is discovered with focus on cryo-EM and X-ray crystallography, and with overview of the emerging XFEL techniques, including single-particle imaging;
- how the accumulated knowledge about the 3D structure of macromolecules has changed our understanding of the chemistry of the processes of life;
- how this knowledge is applied in the development of modern drugs.
- Gale Rhodes, Crystallography Made Crystal Clear, 3rd edition, Academic Press, Amsterdam 2006.
- Bernhard Rupp, Biomolecular Crystallography, Garland Science, New York 2010.
- Arthur Lesk, Introduction to Protein Science, Oxford University Press 2010.
- Carl Branden & John Tooze, Introduction to Protein Structure, 2nd edition, Garland Publishing, New York 1996.