The course aims to provide a deeper understanding of some of the most important experimental methods used to determine the three-dimensional structures of proteins, as a basis for understanding their biological functions. We also aim at an understanding of the forces that underpin the structures of proteins, as well as a basic understanding of the methods used in structure-based drug design.
Upon completion of the course, the participant shall be able to:
- demonstrate good understanding of the three-dimensional structure of proteins, their stability, interactions and dynamics
- explain the theoretical basis for X-ray crystallography
- Perform X-ray crystallography experiments at a basic level, from which the participant can further develop the skills on his/her own.
- demonstrate basic knowledge of how nuclear magnetic resonance (NMR), neutron diffraction and small-angle X-ray and neutron scattering can be used to produce specific information in addition to X-ray crystallography
- assimilate and critically evaluate the scientific literature dealing with protein structure and function, particularly in terms of the experimental methods.
- demonstrate basic knowledge on how structural information can be used in the development of modern Pharmaceuticals
Lectures: Basic knowledge of protein structure: polypeptide conformation. Protein secondary and three-dimensional structure. Stability, dynamics and interactions of proteins: packing and electrostatics. Principles of X-ray crystallography, neutron crystallography, small angle X-ray and neutron scattering. Ligand binding and structure-based drug design.
Laboratory work and computer exercises: Training in the relevant theoretical and experimental methods described for the study of protein structure and dynamics. Includes protein crystallization, data collection at MAX IV, data processing, structure determination and modelling, as well as a simple exercise in ligand docking.
The course is given in the second half of the autumn term. A detailed schedule is under preparation.