Dr. Iva Pritišanac

Proteins are dynamic molecular engines of life, but our understanding of them has long been limited to static snapshots. My research addresses this fundamental ‘blind spot’ in structural biology. The 2024 Nobel Prize recognized the revolution in protein structure prediction (AlphaFold) and pioneering work in computational protein design. However, most state-of-the-art models emerging from these fields are designed for proteins with stable three-dimensional structures. My group focuses on the remaining highly dynamic components of the cellular protein machinery that have eluded traditional structure determination, the so-called intrinsically disordered protein regions (IDRs). IDRs comprise at least a third of the human proteome and often act in concert with structured protein domains. Despite their lack of a fixed conformation, IDRs represent highly dynamic molecular computing machines that integrate environmental signals to program cellular behaviour.

Soon after my PhD at the University of Oxford, where my work relied on stable protein structures, I moved to the University of Toronto and SickKids Research Hospital. There, I worked on constructing a ‘functional map’ of the human intrinsically disordered proteome. This work built a foundation for understanding and predicting the biological roles of thousands of mysterious disordered regions in our proteome, revealing patterns of their impact on cellular interactomes and their involvement in complex pathologies.

At Helmholtz Munich, my lab sits at the intersection of the AI revolution in computational methodologies and high-resolution experimental methods, such as NMR spectroscopy. Our mission is to bridge data-driven modeling and experimental reality by working ‘in a loop’ to iteratively refine both.