Biomolecules Aren’t Rocks: Temperature Sensing and Protein Dynamics

Textbooks and structural models traditionally depict proteins as static, rigid entities. While these snapshots from experimental techniques such as X-ray crystallography and cryo-electron microscopy (cryo-EM) are incredibly useful, they obscure the fundamental reality that life exists in motion. Capturing the full scope and implications of protein dynamics remains a major challenge for experimental and computational techniques alike.

In this Presidential Lecture, Sonya Hanson will discuss the ongoing journey to understand biological temperature sensing — a process that inherently relies on molecules changing shape as a function of small temperature changes. She will highlight how this puzzle has motivated community challenges and methods development to better capture the full conformational landscape of molecules from cryo-EM data. Combined with molecular simulation and recent innovations in machine learning, these technological developments are shifting our focus from rigid structures to dynamic ensembles and refining our ability to see how proteins function.

Hanson joined the Flatiron Institute’s Center for Computational Biology in 2021. Her research focuses on structural and molecular biophysics, particularly the modeling and analysis of experimental data and simulations to understand the molecular mechanisms of key biological processes. She has a B.S. in biophysics from the University of Southern California and received her Ph.D. in biochemistry from the University of Oxford, studying the temperature-sensitive transient receptor potential (TRP) ion channels. Prior to joining the CCB, Hanson was a post-doctoral researcher at the Max Planck Institute of Biophysics, Columbia University, and the Memorial Sloan Kettering Cancer Center. In her research, she combined experimental and computational methods to study temperature-sensitive bacterial sodium channels, extracted continuous conformational heterogeneity from cryo-EM datasets, and how designed better-targeted therapies to kinases.