NEXT EDITION:  July 2024!!

The Call for Applications is presently closed and is expected to open in March 2024.

The course is limited to 16 participants. Decisions on applications should be made by the end of May 2024. Evaluation of applicants respects the principles of offering equal opportunities with regard to gender, disability or ethnicity. 


The structural characterization of proteins, either alone or in complex with relevant ligands, is fundamental to the understanding of biological systems and is at the heart of the drug discovery process. There are many biophysical methods available to study proteins that span from calorimetric techniques to spectroscopic and structural methods, including modeling.

Knowing what a protein looks like in three-dimensional detail enables the optimization of compounds that target it, a concept known as structure-based or rational drug discovery. Membrane proteins, and specifically transporters, play fundamental roles in biochemical processes and are thus one of the most important yet challenging pharmaceutical targets. The main challenges are the structural and functional characterization due to low protein yields and high instability upon removal from their native environment. Fortunately, recent advances in the structural biology field, more specifically in cryo-EM have advanced the field of membrane protein structural biology such that it is possible to obtain high-resolution structures for such challenging targets. Nevertheless, despite these recent advances, significant challenges remain in several steps, especially in sample preparation, stabilization and cryo grid preparation.

This training school aims to increase the skills level of young researchers in structural biology, promoting the integrated approach of state-of-the-art techniques that are usually not covered in the standard university curriculum. The training school encompasses methods like X-ray Crystallography, CryoEMNMRMicro-Scale Thermophoresis (MST), Isothermal Titration Calorimetry (ITC) and Molecular Modeling.

Our main objective is not only to continue to illustrate but also to reinforce the added value of a structural biology approach to the study of proteins. This will be explored from a hands-on perspective, giving emphasis to the limitations and complementarities of the different methods.

ITC and MST will evaluate the affinity and thermodynamics of protein-ligand interactions; NMR studies will include protein-ligand interaction studies with ligands using protein chemical shift perturbation and the ligand observed STD-NMR technique. X-ray Crystallography and CryoEM methods will be used to assess the 3D structure of proteins and derive determinants of molecular interactions. Molecular Modeling will encompass modern theoretical methods and computational techniques used to study protein interactions and the complementarity to the other experimental techniques will be explored.

Besides the hands-on training there will be theory lectures where the main theoretical aspects of each technique will be explained, always with an emphasis on the complementarity with the other techniques.


Photo from the previous edition: