The scientific advances of the last decades have allowed reaching a molecular level understanding of an increasing number of (bio)chemical processes. This state of knowledge is only possible due to the development of numerous methodologies and studies that allow rationalizing, at the atomic level, the relationship between structure and function, and the role of intermolecular interactions in mediating all (bio)chemical processes.

My main research interests are related to the application and development of solution-state nuclear magnetic resonance (NMR) spectroscopy techniques for structural analysis and the study of intermolecular interactions in biological and chemical systems, in the context of functional analysis of catalytic systems and the understanding of molecular recognition processes.

My research has been conducted mainly around three subjects:

- The study of intermolecular interactions in chemical systems relevant to the rationalization of asymmetric transformations or catalysis;

- The study of intermolecular interactions in non-conventional solvents (ionic liquids and CO₂) to rationalize solvation phenomena;

- The study of intermolecular interactions in biological systems for the rationalization of biocatalysis or in the context of drug design.

To explore these research subjects using the NMR technique it is necessary to develop methods that allow obtaining information about molecular structure and dynamics, and interaction mechanisms, in different experimental conditions, such as at high pressure, in heterogeneous mixtures, or highly concentrated solutions of complex composition. Therefore, related research interest has been the development of NMR methods to address these challenges, in particular, high-pressure NMR, diffusion NMR and techniques for the study of protein-ligand interactions.

A recent research theme is the study of intermolecular interactions involving proteins under macromolecular crowding conditions, comparable to those found in vivo. The objective is to better understand the balance between entropic and enthalpic contributions in molecular recognition processes in conditions similar to those found in vivo. This work may have important implications for rationalizing regulatory processes (allostery and signalling) and misfolding of proteins.