Function and structure of surface-bound tau
Zachary Donhauser (Chemistry)
Project Type - B - Flexible: It will be in-person if we are allowed to have URSI students on campus, but it will become a remote project if not.
The microtubule associated protein tau has a variety of important cellular functions, most notably binding to, stabilizing, and organizing microtubules in axons. Tau is also implicated in a host of neurodegenerative disorders such as Pick’s disease, frontotemporal dementia, parkinsonism linked to chromosome 17 and Alzheimer’s disease, which are all characterized by abnormal aggregation of the protein. In spite of significant recent research attention, the full range of tau's normal functions are not completely understood. The overall goal of this project is to build a better understanding of tau’s behavior when it is bound to microtubules, including changes in structure and function that precede pathological aggregation. To achieve this end, this project will investigate the properties of tau when it is bound to solid supports in physiologically-relevant conformations, applying an atomic force microscopy (AFM) based assay that interrogates the protein at the nanoscale.
Prerequisites: Courses desired, but not required: introductory chemistry, biology, and physics.
How should students express interest in this project? Email me with a one paragraph description of why you're interested in the project and how it fits into your overall academic and/or career goals. After reviewing this description, resume, and transcript I will select some students for in person interviews.
This is an 8-week project running from June 7 – July 31