How drugs work, how they target proteins, and how humans can intervene to modulate the underlying biological processes, has always intrigued me. This is why I enrolled to study pharmaceutical science at ETH Zürich (Switzerland), one of the premier research institutions in the world. I found that I was fascinated with the early phase of drug discovery and development, particularly using structure-based drug design. I therefore joined Dr. Emil Pai’s lab at the University Health Network in Toronto (Canada) for an internship, where I was working on fluoroacetate dehalogenases and learned how to use X-ray crystallography. For my Ph.D., I decided to join the group of Prof. Roland Riek in the Department of Chemistry and Applied Biosciences at ETH to become an expert in NMR spectroscopy. There, I successfully solved the Aβ42 fibril structure, which is the main component in plaques found in Alzheimer’s patients. After obtaining my Ph.D., I felt the desire to find new ways of how to interfere with protein aggregation, which if successful is an important route to slow the progression of Alzheimer’s and similar diseases. Thus, I became intrigued with using chaperones to control amyloidogenic diseases, just as nature does. I joined Dr. Marius Clore’s lab at NIH (Bethesda, MD, USA) to expand my knowledge of basic NMR methodologies with one of the world’s experts and to focus on those methodologies geared towards the study of sparsely populated intermediate states which play an outsized role in the aggregation processes.