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Welcome to the Protein NMR Group @ IQFR

The main challenge of the "Protein structure, dynamics and interactions by NMR" 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
1.1. Design and structure-activity relationships in peptides of biomedical relevance
1.2. Molecular basis of the early events triggering protein diseases
1.3. Pathogenic mechanisms of PHOX2B in CCHS
1.4. Host-pathogen interactions
1.5. RNA-binding proteins

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 Protein Design

3. Molecular basis of regulatory processes in the living beings
3.1. Photosensory regulation and signal transduction in bacteria

4. Development and implementation of new NMR methodologies
5. Optimization of protocols for expression and purification of uniformly and specifically labelled proteins