Single-Course English 5 ECTS

Quantitative analysis and modeling in protein science

Overall Course Objectives

The course presents thermodynamic- and kinetic principles and concepts that are commonly used in protein science. We will introduce the theoretical framework for this field, and focus particularly on practical skills for the quantitative analyses of biochemical and biophysical processes. The course will enable the student to formally describe the rates and strength of ligand binding to proteins, as well as the energetics of protein folding and –stability. Other examples include the analysis of protein aggregation and phase separation assays, the interaction of proteins with lipids and nucleic acids
Particular emphasis will be put on the students’ ability to handle, analyse and visualize real world experimental data, to evaluate different theoretical models and to perform statistical analysis. All analysis will be done with Python.

Learning Objectives

  • 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.

Course Content

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.

Recommended prerequisites

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

Teaching Method

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


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.

See course in the course database.





13 weeks




DTU Lyngby Campus

Course code 27330
Course type Candidate
Semester start Week 5
Semester end Week 19
Days Fri 13-17

7.500,00 DKK

Please note that this course has participants limitation. Read more