Chemistry: Structural Biochemistry

<p>Protein interactions are essential for understanding how cells work and these interactions can only be studied by working with the proteins themselves. Dive into the molecular level of the cell and learn more about protein structure and its connection to biological function.</p><p>KEMM35. The overall aim of the course is for the student to acquire an in-depth understanding of proteins, with an emphasis on their three-dimensional structures, the connection of structures to biological function and how these structures are produced. The course covers both the principles that determine the properties of proteins and the most important experimental methods used to study them in modern molecular protein science, such as X-ray crystallography, low-angle X-ray scattering and cryo-electron microscopy. How structural information about proteins can be used to develop better drugs is also discussed.</p> <h2>Course content</h2> <p><em>Lectures</em></p> <ul> <li>Polypeptide conformations</li> <li>Secondary and three-dimensional structures of proteins, structural classes and structure databases</li> <li>Prediction and modelling of protein structure</li> <li>The stability, dynamics and interaction of proteins</li> <li>Ligand bonding and structure-based design of drugs</li> <li>Principles of X-ray crystallography and other methods such as cryo-electron microscopy, Small Angle X-ray scattering, neutron scattering</li> </ul> <p><em>Practical components</em></p> <ul> <li>Exercises in relevant computer-based methods to study protein structures and dynamics</li> <li>Searching in sequence and structure databases, and modelling of proteins of unknown structure</li> <li>Exercises in all critical stages of a typical structure determination using X-ray crystallography: crystallisation, data collection, data processing, structure determination, model construction, refinement and validation</li> <li>Basic exercises using other experimental methods. A number of exercises are carried out as demonstrations</li> </ul>