Dr. Gregory A. Weiss, Professor of Chemistry, Molecular Biology and Biochemistry, University of California (Irvine), USA

Gregory Weiss is a Professor of Chemical Biology. He earned a B.S from UC Berkeley and a PhD from Harvard. His undergraduate and graduate research focused on the development of heterocyclic mimics of peptides. Awarded a Ruth Kirschstein National Research Service Award from the NIH, he returned the funding to pursue post-doctoral studies with Dr. Jim Wells, then at Genentech. In 2000, he joined the faculty at UCI where his laboratory focuses on the interface between chemistry and biology, including studies of enzymes, molecular recognition, and bioelectronics. His awards include Outstanding Professor in the School of Physical Sciences at UCI (elected by the graduating students), Beckman Foundation Young Investigator, and election to Fellow of the American Association for the Advancement of Science. He has published around 100 peer-reviewed articles in chemical biology, biophysics, biochemistry, molecular biology, and organic chemistry. He Co-Founded, and was twice elected Co-Chair of the Global Young Academy, which includes 200 top young scientists from >55 countries. With Dr. David Van Vranken, he co-authored Introduction to Bioorganic Chemistry and Chemical Biology. In 2015, he was awarded the Ig Nobel Prize in Chemistry for leading the team that partially unboiled the egg. He has started two biotech companies, and was UCI’s Entrepreneurial Leader of the Year in 2018. He and his wife, Kim, live in Irvine, California with their three cats.

Speech Title: Listening to Individual Enzymes with Cabon Nanocircuits

Abstract: The Weiss laboratory uses carbon nanotubes to invent new tools for dissecting biology. Specifically, the lab directly wires viruses and individual proteins into carbon nanotube-based electronic circuits, and “listens” to their singing, which occurs when the proteins interact with binding partners and substrates. With collaborator Prof. Phil Collins (UCI), we have spot-welded individual proteins into these electronic circuits, termed “nanophones,” to record the sounds made by proteins in motion. The tethered single molecule can be examined at high-speeds (microsecond resolution) for long durations (up to weeks) in real-time during protein unfolding, folding, binding, and enzymatic catalysis. The approach has been used to dissect the inner-workings of enzymes, including several DNA polymerases and protein kinase A.