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Biomolecular Sciences Seminar Series: Dr. Joan-Emma Shea

Wednesday, Apr. 24 @ 3:00 pm - 4:15 pm MDT

Presenter Information

Speaker: Dr. Joan-Emma Shea, Professor of Chemistry & Biochemistry at UC Santa Barbara

Short Description of Research: Research in the Shea group focuses on developing and applying the techniques of statistical and computational physics to the study of biological problems. Current work involves the investigation of cellular processes such as in-vivo protein folding and protein aggregation.

Seminar Details

Host: Dr. Konrad Meister, Chemistry & Biochemistry

Title: Self-Assembly of the Tau Protein: Liquid-Liquid Phase Separation and Fibrillization

Abstract: Tau is an intrinsically disordered protein that plays an important role in stabilizing microtubules. Under pathological conditions, this protein can also self-assemble into fibrillar structures, a process that has been associated with a class of neurodegenerative diseases known as Tauopathies. Interestingly, this protein is also capable of assembling into liquid droplets through a process of liquid-liquid phase separation (LLPS). Using a combination of field-theoretic simulations, coarse-grained models, and atomistic simulations, we present an investigation of the mechanisms of fibrillization and phase separation of this protein. We investigate fragments of Tau that have a propensity to either phase separate or form fibrils, enabling us to shed light into the sequence characteristics linked with these two modes of assembly. Finally, we introduce a 19-residue fragment of Tau that is capable of seeding the fibrillization of full-length Tau, and we discuss the effect of point mutations in modulating aggregation in familial forms of Tauopathies.

Publication Related to Talk: Tau P301L mutation promotes core 4R tauopathy fibril fold through near-surface water structuring and conformational rearrangement