I6: A Practical Introduction to Biophysical Methods - 34603
(4 days; 2 CP; Spring 2024)
Timothy Sharpe, Tobias Mühlethaler
This course provides a practical and theoretical introduction of a range of biophysical methods that can be used to measure the interactions, stability and size of biomolecules. Students will gain hands-on experience of different techniques, an idea of how those techniques can complement each other, and opportunities to discuss which techniques might be suitable for their own projects.
The techniques covered in the course will be: isothermal titration calorimetry (ITC), microscale thermophoresis (MST), surface plasmon resonance (SPR), differential scanning fluorimetry (DSF), dynamic light scattering (DLS), multi-angle light-scattering (MALS), analytical ultracentrifugation (AUC), and mass photometry.
At the end of the course, students will be required to write a short proposal (2-4 pages) for the application of at least one of the techniques covered in the course to their own research project. The proposal should demonstrate a theoretical understanding of the technique, consideration of the sample requirements and experimental protocol, and ideas about the potential meaning of the results within the context of their project.
Day 1: Overview of methods for biomolecule interactions; Overview of BF resources for users; ITC theory; ITC experiment.
Day 2: MST theory; MST experiment; Overview of other methods for studying binding; discussion of more advanced data analysis (global fitting, error analysis).
Day 3: Overview of stability screening; DSF theory; DSF experiment; DLS theory; DLS experiment
Day 4: Overview of mass and size determination; MALS theory; MALS experiment; Mass Photometry theory and experiment; AUC theory and data analysis.