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.

Angela Irwin is the Klevit Lab Manager. She oversees lab safety, training, purchasing, and helps to keep our lab running smoothly and efficiently.

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.

Coming soon...

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.

As a graduate student, I explored a few polymerases that played roles in either maintaining genetic integrity or the process of adaptation. Exploring further about how nature keeps the genome safe, I got interested in studying the DNA damage repair processes. Genomic alterations in DNA repair enzyme complex BRCA1-BARD1 are implicated in the high risk for the development of breast and ovarian cancers. As a Kleviteer, I am going to survey the BRCA1-BARD1 heterodimeric complex to understand the roles of intrinsically disordered regions (IDRs) accommodated by these giant sister proteins. I will be using biochemical, biophysical and structural tools to advance our knowledge in the field.
When out of lab, I like to play badminton or go out cycling to explore the beautiful Seattle city. On lazy rainy days, I like to spend time doing some mandala art or watch some crazy movies.

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.

My research is focused on the BRCA1/BARD1 E3 ligase complex and its role in the ubiquitination of histone H2A, a process essential for DNA damage repair. I specifically focus on BARD1, working to create various constructs of its intrinsically disordered region to elucidate key features for ligase activity. Additionally, I run our lab website and social media platforms.

Coming soon...

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