domains fold into compact structures stabilized by long-range residue-residue interactions. We study beta-lactamase activity as a micro-evolutive model for the emergence of an enzymatic activity in a globular domain, by locally perturbing the protein sequence and quantifying the changes in protein expression, folding and function. In collaboration with Mario Ermácora.Repetitive protein domains are tandem repeats of similar motifs of 10 to 50 residues. They adopt elongated structures stabilized mainly by local interactions. The parallel between sequence and structure facilitates the description of the energy landscape and sequence space compatible with their function. We use ankyrin repeat domains as models, particularly the I-kappa-B family. In collaboration with Peter Wolynes and Elizabeth Komives

We use maximum entropy models to build systems-level descriptions of the relative abundances of amino acids and codons in organisms. We also build computational models and tools for synthetic biology practicioners. In collaboration with Teresa Krick.Viruses must hijack the molecular machineries of their hosts in order to transcribe, translate and replicate their genomes. Virus-host interactions are often mediated by linear motifs within intrinsically disordered domains. We study the biophysical basis of intrinsic disorder and use information theory to unveil sequence patterns. In collaboration with Gonzalo de Prat-Gay.

We acknowledge funding from Agencia Nacional de Promoción Científica y Tecnológica, CONICET, Instituto Nacional del Cáncer and the National Institutes of Health (NIH).