Pearl is an adjunct teacher, previous postdoctoral fellow, in the Klevit lab where she studies the structures and dynamics of a bacterial adhesion protein called FimH primarily through using NMR. Pearl is fascinated by the unusual properties of FimH including catch-bonds which are molecular interactions that paradoxically strengthen with increasing force and help bacteria evade clearance from the host during flow conditions in the intestinal and urinary tracts. She hopes that her research can aid in developing novel therapeutics to combat bacterial infections that impact communities worldwide. Pearl received her Ph.D. from Johns Hopkins University (Baltimore, MD) and her B.A from Mount Holyoke College (South Hadley, MA). Originally from Uganda, she misses the hot sunny weather, but despite her dependence on cryogen-enabled superconducting magnets she has warmed up to the Emerald City with her trusty space heater underneath her workstation.

I am interested in how intrinsically disordered proteins function as well as their aggregation pathways. My research aims to uncover the mechanisms and kinetics of how small heat shock proteins chaperone the aggregation of amylogenic protein tau. As a co-mentor student in the Klevit and the Nath labs, I use a wide range of biochemical and biophysical techniques to characterize sHSP-tau interactions in depth.

After a PhD focused on the final stages of the ubiquitin transfer cascade, from an RBR E3 ligase to substrate, I became increasingly fascinated with the apparent ‘decision making’ of E2 conjugating enzymes and the impact these enzymes have on the final result of ubiquitin transfer. The field has tremendous knowledge of the E2 impact on linkage type, site preference, mono- or poly-ubiquitylation, chain elongation, etc. However, the underlying reaction chemistries of ubiquitin transfer and how small changes between members of the highly conserved E2 family influences this is still largely unknown. Through biochemical and biophysical techniques, I will examine both well-known and uncharacterized E2s to expand our insight into what, at the most basic level, makes these enzymes work.

Maria’s interests are focused on two areas of protein research: 1) protein aggregation inhibition by chaperones and 2) intrinsically disordered proteins. She likes it best when these two are intertwined, which is exactly what she loves about small heat shock proteins. As she gets easily bored, she likes to try new methods and think of new ways to answer hard questions (which fits well since small heat shock proteins do not succumb easily to classical biochemistry methods). When she is not at work she enjoys the beautiful Pacific Northwest, either skiing or hiking, and when stationary at home she smokes meat and sings her heart out to the sound of her guitar.

I am a recent graduate from Western Washington University where I studied Biochemistry and worked in an organic synthesis laboratory. I joined the Klevit lab to learn more about biochemistry in a lab setting, and I am excited to start working on the BRCA1/BARD1 project.

My research is aimed at characterizing the noncanonical yeast E2 Ubc6. I investigate its mechanism for ubiquitin discharge and attempt to identify critical residues between the E2 and Ub involved in coordinating this chemical reaction using NMR spectroscopy and in vitro enzymatic functional assays.

I am interested in characterizing the N-terminal interactions of the small heat shock protein aB-crystallin through NMR and other biochemical techniques in order to better understand their contribution to the oligomerization and client binding of said protein. I also work on creating new constructs of aB-crystallin and related small heat shock proteins for study in our lab. Along with Thomas, I also manage the lab, handling purchasing, training, lab safety, and other miscellaneous tasks.

Lisa is a staff scientist in the Klevit lab. She manages the various lab instruments including the Magnets, SEC-MALS, CD, and fluorometer. Her research interests include fuzzy complexes formed by IDRs and their binding partners, specifically those involved in transcription regulation