I6: A Practical Introduction to Biophysical Methods (BF Course) – 34603
(4 days; 2 CP; Spring 2021)
Ludovit Zweifel, Timothy Sharpe
This four-day course provides a practical and theoretical introduction of a range of biophysical methods that can be used to measure the stability, size, interactions and dynamics 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), analytical ultracentrifugation (AUC), dynamic light scattering (DLS), multi-angle light-scattering (MALS), fluorescence correlation spectroscopy (FCS), and fluorescence lifetime imaging (FLIM).
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: Theory of binding interactions; ITC and MST experiments.
Day 2: Other methods to study binding; Advanced data analysis; Theory of proteinstability; DSF experiments.
Day 3: Theory of mass and size determination; AUC data analysis; DLS and MALS experiments.
Day 4: Theory of time-resolved fluorescence imaging; FCS and FLIM experiments.