Danielle Tullman-Ercek Developing methods to interrogate the interplay of sequence, geometry, and function for multi-protein systems
Research Interests
Highly organized self-assembling proteins abound in the living world, and the resulting assemblies govern critical processes at all levels of life, from the formation of virus capsids to the transport of oxygen in the blood. The Tullman-Ercek lab is interested in several questions related to self-assembling systems: 1) What fundamental principles govern the precise organization of proteins at the nanoscale? 2) How does organization of biochemical processes enhance their performance? 3) How can we manipulate these protein assemblies to gain new or enhanced functions in living systems? Answering these questions permits advances in a wide range of application spaces, including vaccine development, manufacturing of therapeutics, and sustainable chemical production. Our current model systems include protein containers such as the MS2 viral capsid and bacterial organelles called microcompartments, and membrane protein machines such as the type III secretion system and multidrug efflux pumps. In the process of trying to engineer these systems to gain or improve function, we often make surprising observations that lead to new, hypothesis-driven inquiries. Our current work focuses on engineering new vaccine scaffolds, therapeutics, and sustainable biochemical production.
Selected Publications
Self-assembling protein materials with genetically programmable morphology and size. Miller JB, Abrahamson CH, Lee MS, Palmero BJ, Kennedy NW, Mills CE, Tullman-Ercek D. ACS Nano. 2025 November 21;19(48):40917-40931
View all publications by Danielle Tullman-Ercek in the National Library of Medicine (PubMed). Current and former IBiS students in blue.
