Danielle Tullman-Ercek Engineering of membrane proteins & protein membranes

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, cancer therapeutics, and microbial biochemical biosynthesis processes.

Selected Publications

Quantitative characterization of all single amino acid variants of a viral capsid-based drug delivery vehicle. Hartman EC, Jakobson CM, Favor AH, Lobba MJ, Álvarez-Benedicto E, Francis MB, and Tullman-Ercek D. Nature Communications. 2018 April 11;9:1385.

Evolutionary engineering improves tolerance for medium-chain alcohols in Saccharomyces cerevisiae. Davis López SA, Griffith DA, Choi B, Cate JHD, and Tullman-Ercek D. Biotechnology for Biofuels. 2018 April 2;11:90.

Evidence for Improved Encapsulated Pathway Behavior in a Bacterial Microcompartment through Shell Protein Engineering. Slininger Lee MF, Jakobson CM, and Tullman-Ercek D. ACS Synthetic Biology. 2017 October 20;6(10):1880-1891.

Proteins adopt functionally active conformations after type III secretion. Metcalf KJ, Bevington JL, Rosales SL, Burdette LA, Valdivia E, and Tullman-Ercek D. Microbial Cell Factories. 2016 December 23;15:213.

A Selection for Assembly Reveals That a Single Amino Acid Mutant of the Bacteriophage MS2 Coat Protein Forms a Smaller Virus-like Particle. Asensio MA, Morella NM, Jakobson CM, Hartman EC, Glasgow JE, Sankaran B, Zwart PH, and Tullman-Ercek D. Nano Letters. 2016 September 14;16(9):5944-5950. 

View all publications by Danielle Tullman-Ercek in the National Library of Medicine (PubMed).