University of Michigan
Q: What field is your PhD in? How did you specialize in biophysics?
My PhD is in biophysics. I originally focused on computational and theoretical chemistry as an undergraduate. As I matured, I realized my interest was more in the experimental side.
Q: What is your current research project?
Currently, most of our work focuses on misfoldedproteins called amyloids. Amyloid proteins are a very hot topic now, as they are both poorly understood and linked to many common degenerative diseases such as Alzheimer’s and Parkinson’s. Our lab focuses on two in particular. IAPP, which is linked to loss of insulin producing beta-cells in type II diabetes, and SEVI, an amyloidogenic protein which has a role in HIV infection. Neither of these proteins has been intensively studied as the Aβ protein involved in Alzheimer’s, and it is interesting to see how far we can generalize models specifically made for the Aβ protein to other proteins.
Q: What initially attracted you to the field?
The possibility of seeing hidden connections between seemingly unrelated phenomena. The amyloid proteins we are studying are a good example of this. We are finding that if they are looked at from the perspective typically used in polymer and soft matter physics, instead of the traditional biochemistry approach, many aspects that seemed unclear are suddenly illuminated.
Q: What skills and experiences have you gained from your postdoc position?
In my experience, the main difference between postdoc and graduate training is project management. After graduate school, you have many technical skills but have to learn what types of research problems are feasible and how they may be best approached.
Q: Tell us about a great experience or opportunity you’ve had in the past year?
The Biophysical Society meeting was great. In my poster session the person after me did not show up, which was lucky, as I was able to take more questions from the audience than is normally allowed. We were also able to solve one of the first high-resolution structures of prefibrillar Aβ1-40 this year, which showed a very different structure than what was expected (Protein Databank number 2LFM).
Q: What do you hope the next step in your career path will be?
I’m currently applying for assistant professor positions.
Q: Why did you join the Biophysical Society?
The Annual Meeting is an important event for our group. It allows us to present our research to wider audience, some of whom may not be aware of our research otherwise. Similarly, the meeting makes us aware of much research we would not normally be aware of.
Q: If you were not a biophysicist, what would you be?
I can’t imagine doing anything else.
Ayyalusamy Ramamoorthy, Brender’s PI says:
Jeff has been working in the biophysical aspects of misfolding of amyloid proteins and their implications in aging-related amyloid diseases. He has contributed significantly to this field and has published more than 30 peer-reviewed articles in top in top journals. He is also creative and dedicated to research.
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