The nuclear magnetic resonance (NMR) group, under leadership of Prof. Jiménez Barbero is interested in the development of general methodological aspects of the NMR techniques and, particularly, in their applications to the study of the conformation and dynamics of the molecular recognition processes. During the last few years we have determined the solution 3D structure of different proteins using a protocol based on NMR spectroscopy, assisted by molecular mechanics and dynamics calculations. This methodology has been applied to different carbohydrate molecular complexes of wild type and mutant lectins, glycosidases, and to the elucidation of the structure of other protein receptors of biomedical interest. We have investigated protein complexes with natural ligands and with synthetically modified analogues. We have also investigated the structural characteristics, both from the conformational and dynamical point of view of different biologically relevant oligo and polysaccharides also using NMR and molecular dynamics. In particular, we have paid attention to the physic-chemical origin of the interaction between carbohydrates and proteins, with special emphasis in the relative role of sugar-aromatic stacking interactions. Natural abundance as well as labeled ligands and proteins (13C, 15N) have been used for these studies. Thanks to the collaboration with several research groups throughout the world, some studied systems include galectins, hevein domains, ricin-B, viscumin, lactase, E. coli beta-galactosidase, Streptomyces Sp. beta-glucosidase, ribonuclease B, DC-SIGN, acidic fibroblast growth factor, cholera toxin B, HexS1 homeodomain, glycomimetics, C- and S-glycosyl compounds, aminoglycosides, carbohydrate antigens, bacterial and fungal polysaccharides, etc. This last research line overlaps with a, still alive, old one of the group, aimed at establishing the structural basis of the inhibition/activation of fibroblast growth factor, a protein deeply involved in important pathologies, and at designing inhibitors of its mitogenic activity Prof. Giménez-Gallego and Dr. Lozano).These studies require relatively simple studies of cell biology sometimes. The group is also interested in establishing the structural basis of the biological activities of certain virulence factors of Streptococcus pneumoniae and in designing inhibitors against bacterial virulence (Prof. Giménez-Gallego, Dr. Romero). Once the three-dimensional structure of the choline-binding domain of the pneumococcal autolysin LytA has been solved by X-ray diffraction by the group, they have proceeded to identify low molecular-mass compounds which may lead the design of inhibitors of this enzyme. Dr. Romero’s laboratory is also interested in the determination of the enzyme UDP-glucose pyrophosphorylase, a key component of the pneumococcal cell capsule in all the known strains of this bacterium. The group is also undertaking now the structural characterization of the insulin growth factor binding proteins, a family of polypeptides involved in numerous crucial physiological functions and pathologies. The group collaborates with numerous Spanish and foreign research laboratories in numerous other projects not directly related with its main research goals.