Protein Folding and Assembly, from molecule to disease


About this course

Structural biology centers on the chemical principles underlying protein structure and function. A particular focus is the assembly of biomolecules into molecular machines and the biomolecular processes that are controlled by those machines. The folding and assembly of proteins into molecular machines is one of the great integrating themes related to key questions in today’s life sciences: How can molecules assemble almost error-free into complex machines? How can molecular chaperones guide these processes? Some molecules never fold – why? What happens to proteins when they are damaged? What happens when protein aggregate, and why do we die because of this? Are there strategies to develop molecular therapies against protein folding diseases, such as Alzheimer, Parkinson or mad cow disease?

We will explore how proteins “know” what shape they should fold up into following their synthesis, how they cluster into dynamic macromolecular complexes, and how these complexes communicate to form “social” networks that enable cells to move, replicate, signal, and execute other vital processes. The course is accompanied by research-oriented practicum experiments and complimented with lectures.

Students will be trained to develop and write a research proposal on a related topic, ideally as preparation for their bachelor thesis.

Learning outcomes

  1.  Theoretical and practical skills in key techniques to study biomolecular complexes (protein biochemistry, fluorescence and NMR spectroscopy, radioactive pulse labelling techniques).  
  2.  Insights how research laboratories apply structural techniques to get insights into biomolecular processes.  
  3.  Knowledge and skills to understand and judge the experimental part of research articles in structural biology.  
  4.  Skills for conceiving an interdisciplinary grant proposal in the area structural biology.  

Objective of the course
At the end of this course you will have acquired sufficient knowledge for understanding and evaluating interdisciplinary research articles in protein science. You will have an overview of the available methods for characterising biomolecules and interactions between biomolecules, in vitro and in the living cell. Furthermore, you will have gained an insight into the way research laboratories formulate and study hypotheses, and you will be able to develop interdisciplinary project plans for analysing biomolecules. The aim of the course is to provide students with intellectual and technical skills to as excellent basis for a master programme in the molecular life sciences.

Required prior knowledge

Third year Chemistry and MBLS students who have finished the compulsory part of their curriculum have the required prerequisite knowledge. Other motivated students (e.g. second year Chemistry and MBLS students; and UCU students, internationals etc.) are welcome to register, but only after contacting the course coordinator for a personal check of their background knowledge.

Link to more information

If anything remains unclear, please check the FAQ of Utrecht University.


  • Start date

    3 February 2025

    • Ends
      11 April 2025
    • Term *
      Period 3
    • Location
    • Instruction language
    Currently no more seats available
These offerings are valid for students of TU Eindhoven