Biophysics and biophysical chemistry
Overall Course Objectives
In this course we will work with fundamental physical and physico-chemical principles that are commonly used within life science.We introduce basic theoretical frameworks for analyses of e.g. protein stability, ligand binding, enzyme kinetics and biotech applications of microscopy and spectroscopy.
The overarching goal is to enable the student to make practical use of these tools within a broad range of quantitative analyses in life science.
See course description in Danish
Learning Objectives
- Describe the meaning and use of internal energy, enthalpy, entropy, Gibbs free energy and chemical potential.
- Solve problems using the principle of state functions.
- Explain the thermodynamic basis for colligative properties especially osmotic pressure.
- Solve problems related to chemical equilibrium and describe its dependency on temperature and pressure.
- Describe intermolecular interactions, which are essential for protein structure and ligand binding.
- Analyse the dynamics of ligand binding
- Model enzyme reactions and identify rate limiting steps
- Explain principles and applications of fluorescence spectroscopy
- Apply fundamental optical spectroscopy within life science research
- describe the electric potential of the cell membrane and its role for nerve signals
Course Content
This course uses short e-lectures which can be found at DTU LEARN and it is expected that the students have watched relevant e-lectures before each session. The e-lectures provide a short introduction to the different topics and make reference to more detailed treatments in the book (or supplementary information on DTU LEARN). In class there will be a short introduction to the topic by the teacher, and the main activity will be group work and exercises in smaller groups and student presentations. The groups will also work with case-stories that analyses biochemical and biophysical data.
The course covers three areas: thermodynamics, kinetics and biophysics. In thermodynamics, we will work with selected topics in Part 1 of the textbook. This includes the application of the functions enthalpy and free energy for the description of protein stability and ligand binding. In kinetics, we will work with part 2 of the textbook and introduce formal rate equations within life science. We will analyze experimental data from pharmacokinetics, enzyme kinetics and the dynamics of ligand-receptor interactions. In the last part – biophysics – we study interactions between light and biomolecules (spectroscopy and microscopy) as well as the formal description of electric potentials across cell membranes.
Possible start times
- 6 – 20 (Fri 8-12)
Teaching Method
e-lectures, lectures, case-stories, data analysis and exercises.
Faculty
Limited number of seats
Minimum: 10.
Please be aware that this course will only be held if the required minimum number of participants is met. You will be informed 8 days before the start of the course, whether the course will be held.



