Dr. Pau Bernadó is a Professor of Structural Biology at Centre de Biologie Structurale (CBS), a joint research unit of CNRS, INSERM, and University of Montpellier in France. His research program focuses on intrinsically disordered proteins (IDPs) and protein conformational ensembles, utilizing integrative structural biology approaches with particular emphasis on Small-Angle X-ray Scattering (SAXS) techniques combined with computational modeling. Dr. Bernadó's research interests include: Structural characterization of intrinsically disordered proteins Development of computational tools for analyzing protein conformational ensembles Protein-protein interactions in flexible systems Structure-function relationships in protein homorepeats Integrative structural biology methodologies His recent work has centered on developing advanced computational approaches like WARIO and WASCO for characterizing conformational ensembles of highly flexible proteins. The research spans fundamental protein science to understanding disease-related proteins and viral components. With over 110 scientific publications including numerous high-impact papers in journals such as Nature Communications, PNAS, and Nucleic Acids Research, Dr. Bernadó has established himself as a leading researcher in the field of protein structural dynamics. Notable scientific contributions include: Development of computational tools for IDP analysis (pyDockSAXS, WARIO, WASCO) Advancement of SAXS methodologies for studying flexible proteins Major contributions to the Protein Ensemble Database (PED) Structural insights into protein homorepeats and their disease relevance Methodological innovations for studying low-complexity protein regions Dr. Bernadó maintains active collaborations with researchers across Europe and supervises students and postdoctoral researchers in structural biology and biophysics. His lab provides interdisciplinary research opportunities at the interface of experimental and computational structural biology, with particular focus on understanding the dynamic nature of protein structure and function.






