Julie Forman-Kay: Dynamic views on protein structure

JCB • VOLUME 214 • NUMBER 6 • 2016 638 Julie Forman-Kay became fascinated with the dynamics of biological systems early on: in grade school, she fell in love with science when she had to observe the metamorphosis of mealworms into adult insects. Her interest in biological dynamics grew stronger and more molecular during her undergraduate studies in chemistry at MIT, where she worked with famed biophysicist Alexander Rich, biochemist Lee Gehrke, biotechnology pioneer Robert Langer, and crystallographer Gregory Petsko. In particular, her time in the Petsko lab, where she was directly supervised by Stephen Burley and also interacted with John Kuriyan (now at Rutgers and UC Berkeley, respectively), set her on the path of combined experimental and computational structural biology. For her doctoral studies, Forman-Kay set out to study the structure of the disordered fragments of the bacterial protein thioredoxin with Fred Richards at Yale. With sample aggregation plaguing the project, Julie switched to determining the structure of human thioredoxin by NMR near the end of her PhD and continued during her postdoc in the joint lab of Angela Gronenborn and Marius Clore at the NIH. With these critical NMR skills, she set up her lab at The Hospital for Sick Children. In one of her fi rst projects, she conducted a structural study of a folded SH3 domain from the Drk signaling protein. She found that the folded state exchanged with its disordered unfolded state and was able to characterize the fl uctuating structure that allowed folding and stability. In essence, she was able to accomplish her PhD thesis goals, an ironic twist of fate that she recalls describing to Fred Richards when visiting Yale years later. Her lab developed several methods applicable to intrinsically disordered proteins to understand the interplay between dynamics, disorder, and function. We contacted her to learn more about her work and career.