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.

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, CryoEM, NMR, SAXS, Carbohydrate Microarrays, Micro-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.

Carbohydrate Microarrays will identify candidate ligands and analyze the carbohydrate-binding specificity; 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, CryoEM and SAXS 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: