Quantitative analysis and modeling in protein science

• Analyze the rate and strength of ligand binding from data obtained with a variety of different methods.
• Identify spontaneous and non-spontaneous biochemical processes.
• Evaluate thermodynamic and kinetic stability of protein conformations.
• Assess enthalpic- and entropic contributions to the driving force for folding and binding.
• Discuss intermolecular forces that drive protein interactions.
• Understand diffusion and quantify diffusion rates.
• Model multi-step enzyme reactions and identify rate-limiting steps.
• Understand energy landscapes for catalysis and folding (including the effects of mutations).
• Analyse kinetic data of protein aggregation.
• Understand the basics of statistical thermodynamics applied to protein folding and interactions.
• Analysis the thermodynamics of liquid-liquid phase separation of proteins.
• Perform linear and non-linear fitting of experimental data sets.

The content will cover both kinetic aspects (enzymes, aggregation) as well as thermodynamics (ligand binding, protein folding, protein-protein interactions, phase separation) of protein reactions. Some aspects, such as protein folding will be partly discussed with the help of toy models, but overall the emphasis will be on the analysis of real world data from the literature or our own research projects. The students will be equipped with a very large tool kit to quantitatively analyse basically any relevant type of interaction that proteins can undergo, both from the kinetic and thermodynamic standpoint.

26211/27022, Biochemistry, or a comparable course in basic biochemistry
Basic physical chemistry/thermodynamics

Lectures, recorded lectures, case stories, problem solving, data analysis

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.