A world leader in elucidating the relationships between structure, dynamics and function of intrinsically disordered proteins and biomolecular phase separation.
Julie Forman-Kay received a BSc in Chemistry from MIT in 1985 and a PhD from Yale in 1990, followed by post-doctoral training at the NIH. In 1992, she joined The Hospital for Sick Children (SickKids), where she is now the Program Head of the Molecular Medicine research program. She holds a cross-appointment in the Biochemistry Department at the University of Toronto.
The Forman-Kay lab uses NMR and computational methods to better understand the dynamics of intrinsically disordered proteins. Her pioneering studies of the Sic1:Cdc4 complex changed our view of what a protein interaction is and set the stage for the idea that dynamic multivalent interactions can drive liquid-liquid phase separation. She is now exploring how phase separation involving disordered proteins regulates the cellular organization and biological function, focusing on the biophysics and biochemistry of biomolecular condensates. Her work demonstrated in particular that disordered regions of RNA-binding proteins phase separate to create condensates that regulate enzymatic reactions and that post-translational modifications and charge effects control this phase separation. Her group has also characterized the functional dynamics, disease mechanisms, and drug binding of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel. The Forman-Kay lab develops computational tools to describe ensembles of disordered protein structures and predictors of phase separation and, in collaboration with Alan Moses, bioinformatics approaches for disordered protein regions based on features rather than positional alignment.
Dr. Forman-Kay holds a Canada Research Chair in Intrinsically Disordered Proteins; was awarded the 2012 CSMB Jeanne Manery Fisher Memorial Lectureship and the 2013 Zellers Senior Scientist Award from Cystic Fibrosis Canada; and was named a Fellow of the Royal Society of Canada in 2016 and of the Royal Society (London) in 2021.

A pioneer in the communication of human proteins and viral nucleic acids central to viral infection.
Trushar Patel obtained a BSc (2000) and an MSc (2002) in Biotechnology from India. He joined the University of Nottingham in the UK for his PhD (2007), where he studied solution structure and interactions of plant polysaccharides. Subsequently, he joined the University of Manitoba in Canada, working on the structures of human extracellular matrix proteins. Dr. Patel started his career as an independent researcher at the University of Lethbridge in 2016.
Dr. Patel uses interdisciplinary approaches to study the interaction of viral nucleic acids with host proteins - an interaction at the heart of viral infections. Information on the specific sites of host proteins that communicate with viral nucleic acids will ultimately allow the development of therapeutics that prevent host-viral communication. These interactions are essential for the survival and replication of the virus - stopping the interactions is thus of benefit for treating viral infection.
Dr. Patel holds a Tier 2 Canada Research Chair in RNA and Protein Biophysics. He is also one of the editors of the European Biophysics Journal. His work was supported by postdoctoral fellowships from the Manitoba Institute of Child Health (2008) and the Canadian Institutes of Health Research (2010). He also received the Marie Sklodowska-Curie fellowship (2013) from the European Union. He has been very active in training the next generation of researchers, as well as with scientific and science-policy-related conference organizing activities.

Cees Dekker is Distinguished University Professor at Delft, and KNAW Royal Academy Professor. Trained as a solid-state physicist, he discovered many of the exciting electronic properties of carbon nanotubes in the 1990s. 20 years ago, he moved to single-molecule biophysics and nanobiology. His recent research is on nanopores for sequencing and nuclear transport, chromosome biology, and synthetic cells.

Ruth Nussinov is at Frederick National Laboratory for Cancer Research. Her group aims to elucidate the detailed mechanisms of key protein nodes in oncogenic signaling pathways of receptor protein kinases (RTK), centering on upstream regulation and downstream activation and communication of Ras signaling pathways. She is an Elected Fellow of the American Physical Society, the AIMBE (Medical and Biological Engineering), the Biophysical Society, and the ISCB. She won many Awards, and has been a frequent Keynote speaker in domestic and international meetings. She was the Editor-in-Chief of PLOS CB, and currently is Editor-in-Chief of Current Opinion in Structural Biology.

Sandra Schmid’s highly collaborative laboratory at the Scripps Research Institute (1988-2011) and then UT Southwestern (2011-2020), applied cell and molecular biology, biochemistry, biophysics, structural biology, and quantitative live cell microscopy to define the molecular mechanisms underlying clathrin-mediated endocytosis; with particular focus on the paradigmatic fission GTPase, dynamin. Schmid’s work, published in over 170 articles and reviews, has been recognized by numerous awards, including her election to the National Academy of Sciences in 2020. She currently serves as the inaugural Chief Scientific Officer of the Chan Zuckerberg Biohub.

Sriram Subramaniam is the Gobind Khorana Canada Excellence Research Chair in Precision Cancer Drug Design at the University of British Columbia. Dr. Subramaniam's research team uses high-resolution cryo-EM imaging of native protein complexes to design effective therapeutic agents targeting key drivers of diseases such as cancer, infectious diseases and brain disorders. His lab also develops next generation technologies in cryo-EM and related methods using automated workflows coupled with advanced image processing and machine learning. Dr. Subramaniam's research has led to major advances including the world’s first molecular-level structural analysis of the Omicron variant spike protein. His contributions have been recognized by recent major awards and nominations including the National Cancer Institute Research Highlights Award (2013), Federal Technology Transfer Award (2015), NIH Director’s Award for Scientific Excellence (2015), Orloff Award from NHLBI, NIH for outstanding scientific contribution (2016), election as Fellow of the Biophysical Society (2018), and nomination for the Breakthrough Prize in the Life Sciences.