David Fushman

David Fushman is an Adjunct Professor affiliated with the Institute for Physical Science and Technology (IPST) and holds a joint appointment in the Department of Chemistry & Biochemistry and the Institute for Advanced Computer Studies (UMIACS) at the University of Maryland. His research focuses on understanding proteins as dynamic molecular machines at atomic resolution, particularly investigating structure, dynamics, and recognition in multi-domain proteins and complexes. Central themes include intracellular signaling via ubiquitin-mediated pathways, with emphasis on methodologies like nuclear magnetic resonance (NMR), small-angle X-ray/neutron scattering (SAXS/SANS), and molecular dynamics simulations. His work bridges biophysics, biochemistry, and computational biology, addressing fundamental questions in protein function and disease mechanisms.

Recent studies highlight discoveries in ubiquitin signaling mechanisms, including selective recognition of polyubiquitin chains by macrocyclic peptides and the structural basis of ubiquitin’s CO₂-binding capacity. His lab integrates advanced imaging and computational tools to probe protein dynamics in health and disease contexts such as cancer and neurodegeneration. Key contributions include structural insights into SARS-CoV-2 protease interactions and development of GenApp-based science gateways for NMR data analysis.

Grants include NSF-funded research on ubiquitin-Rub1 cross-activation. His interdisciplinary approach fosters collaborations across physical and life sciences, driving innovations in structural biology and therapeutic target identification.