معرفی
David Jacobson is an Assistant Professor in the Department of Chemistry, College of Science at Clemson University. His research group uses single-molecule force spectroscopy to study membrane-protein folding and energetics, with support from the NSF CAREER Award.
Education:
- B.A., Biochemistry & Physics, University of Pennsylvania, 2011
- Ph.D., Physics, University of California, Santa Barbara, 2016
Research Interests:
Dr. Jacobson’s lab focuses on the physical chemistry and biophysics of membrane proteins. By applying precisely controlled forces with atomic force microscopy (AFM), the group measures how individual membrane proteins unfold and refold. These measurements allow thermodynamic characterization of protein stability as a function of ligand concentration, disease-causing mutations, and lipid environment. The work bridges fundamental physical chemistry with biomedical questions surrounding drug targets and protein-misfolding diseases.
Scientific Awards:
- NSF CAREER Award (2025-2030)
- NIH K99/R00 Pathway to Independence Award (2021-2026)
- APS DBIO Award for Outstanding Doctoral Thesis Research in Biological Physics (2017)
- NIST NRC Postdoctoral Research Associateship (2017-2019)
- NSF Graduate Research Fellowship (2013-2016)
- Chair's Award, Biochemistry Program, University of Pennsylvania (2011)
- Roy and Diana Vagelos Molecular Life Science Program, University of Pennsylvania (2007-2011)
Teaching & Mentoring:
Dr. Jacobson teaches core physical-chemistry courses including Introduction to Physical Chemistry (CH 3300), Physical Chemistry II (CH 3320), and a special-topics graduate course on Scanning Probe Microscopy (CH 9300). The lab actively recruits both undergraduate and graduate researchers, welcoming new Ph.D. students such as Carrie Baumgardner (medical-biophysics) and Alex Lybrand (chemistry).
Laboratory Facilities:
The Jacobson Lab is housed in Hunter Hall at Clemson University, with office space in rooms 157 and 373, and experimental laboratories in rooms 436 and 443. The group specializes in custom atomic force microscopy instrumentation for single-molecule force spectroscopy studies of membrane proteins.
