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The general objective of the "Protein structure, dynamics and interactions by NMR" Group is the elucidation of the physicochemical bases that determine the structure, dynamics, stability and folding properties of peptides, proteins, nucleic acids and their complexes. This information is essential for a detailed description of their biological function. To that end, we use mainly high resolution multidimensional nuclear magnetic resonance (NMR) spectroscopy. More specifically, the following research lines are addressed:

Development of new NMR methodology for fast and highly efficient determination of three-dimensional structures of biomacromolecules and their complexes.

New methods to study proteins of large size and their complexes under conditions similar to those prevailing in vivo.

New methods to study IDPs (intrinsically disordered proteins) and detection of structural tendencies.

Design of peptides with well-defined conformations. Structure-activity relationships.

Protein folding: pathways, intermediates and kinetics.

Structural study of proteins of biomedical relevance: applications in cancer, allergy, amyotrophic  lateral sclerosis (ALS), memory consolidation and dementia such as Alzheimer's disease.

 
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