Group of Protein NMR spectroscopy
The main challenge of the "Protein NMR spectroscopy" Group is understanding the structural bases of life. Our general aim is to elucidate the physicochemical principles that determine the structure, dynamics, stability, folding and recognition of peptides, proteins, and nucleic acids, with a particular focus in disease-related biomolecules. 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 and get additional data from various biophysical techniques as well as from computational methods. Currently, our research lines are the following, contributing with the last two to facilitate and speed all others:

1. Structure, dynamics, stability and recognition in proteins and peptides of biomedical relevance
1.1. Design and structure-activity relationships in peptides of biomedical relevance  
1.2. Mechanisms of molecular recognition in RNA-binding proteins involved in human health
1.3. Molecular basis of the early events triggering protein diseases 
1.4. Pathogenic mechanisms in rare diseases: the case of PHOX2B in CCHS 
1.5. Photosensory regulation and signal transduction in bacteria
1.6. Proteins formed by Polyproline II helices for Protein Design
1.7. Regulation of transcription termination in Eucaryote
1.8. Structure and interactions in proteins of interest as potential therapeutical targets 
1.9. Structural biology of host-pathogen interactions in SARS-CoV-2 and other virus

2. Intrinsically disordered proteins and phase transitions (monomer-to-condensate and monomer-to-amyloid)
2.1. Characterization of Intrinsically Disordered Proteins from Coronavirus SARS-CoV-2 
2.2. Homo & hetero-oligomeric foldomes of functional and pathological amyloids 
2.3. Polyproline II Helices in Biomolecular Condensates and for amyloid formation

3. Development and implementation of new NMR methodologies

4. Optimization of protocols for expression and purification of uniformly and specifically labelled proteins