Research

Disordered proteins as sensors and actuators

Disordered proteins do not have a fixed three-dimensional form, and exist instead as an ensemble of rapidly interconverting conformations. This makes them sensitive to even mild changes in the physical-chemical environment of the cell. Yet how even routine changes to the cellular environment affect disordered proteins remain unknown. Our lab is developing methods to understand how routine events (i.e. cell cycle changes) or pathological conditions (e.g. metabolic changes in cancer) alter the dynamics and function of disordered proteins.

Key publications: Hunter, Brandt et al. Nature 2026; Moses, Guadalupe et al. Nat. Struct. Mol Biol 2024.

Protecting proteomes from stress

Countless organisms experience environmental stress as part of their life. Evolution has developed remarkable mechanisms to protect these organisms. We focus on proteomic protection: the ability to prevent irreversible protein damage during routinely occuring abiotic stress events such as dehydration, excessive temperatures, or oxidative damage. Specifically, we examine the physical-chemical principles underlying evolved tolerance, as well as endogenous protectants found across all kingdoms of life.

Key publications: Romero-Perez et al. Cell Systems 2025; Romero-Perez et al. Chem. Rev. 2023.

Environmental control of the biophysical properties of condensed protein phases

Recently, the ability of proteins to form condensed phases has been shown to be critical for various crucial cellular functions. This tendency for phase separation is modulated by a delicate balance between protein structure and the cellular environment, altering the physical and chemical properties of the condensed phase, and the behavior of the proteins that must function within these phases. We look at how changes in the surrounding solution alter the ability of proteins to form specific, functional, and stable condensates.