Jenny Cappuccio
Dr. Cappuccio is interested in how membrane and surface proteins interface on the nanoscale. The research encompasses the biochemical and biotechnology aspects of these two classes of proteins, focusing on understanding their interactions with lipids and other proteins. Student use nanotechnology tools to enable studies of GPCRs such as the CB2 receptor and other membrane proteins in lipid nanodiscs. New areas of research include investigations of novel cellulases in partership with CSUPERB and the Joint Genome Institute and applications of membrane proteins in stem cell biology. Students are introduced to microbiology techniques, protein expression tools, sequencing and DNA isolation as well as in depth protein biochemistry and analysis. Students conduct research and have the opportunity to present their research.
Specialty Area
Biochemistry, Biotechnology, Nanobiotechnology. Membrane Proteins in cluding G-protein Coupled Receptors, and Surface Proteins. Cellulases Bioenergy and Bioremediation. Stem Cell Biology. Student Success. Active Learning. Inclusive Teaching.
Education
2010-2013 - Project Scientist, Lawrence Berkeley National Laboratory - The Molecular Foundry (Nanobiology and Biochemistry)
2006 - 2010 - Postdoctoral Scholar, Lawrence Livermore National Laboratory (Nanobiology and Biochemistry)
2004 - Ph.D., University of California, Santa Cruz (Biochemistry)
1997 - B.S., California State University, Chico (Biochemistry)
Courses Taught
Seminar in Chemistry (CHEM 485)
Biochemistry (CHEM 434/434L & CHEM 435/435L)
Brief Biochemistry (CHEM 438)
General Chemistry (CHEM 109)
Supervised Internship (BIOL 485)
Selected Topics in Biology (BIOL 580)
Publications
12. Coleman MA†, Cappuccio JA†, Blanchette CD, Gao T, Arroyo ES, et al. (2016) Expression and Association of the Yersinia pestis Translocon Proteins, YopB and YopD, Are Facilitated by Nanolipoprotein Particles. PLOS ONE 11(3): e0150166. https://doi.org/10.1371/journal.pone.0150166 † contributed equally
11. J. A. Cappuccio, M.J. Sarachine Falso, M.Kashgarian ; B.A. Buchholz. “14C Analysis of protein extracts from Bacillus spores,” Forensic Sci. Int., 2014, 240, 54-60. https://doi.org/10.1016/j.forsciint.2014.04.003
10. Blanchette, C., J. Cappuccio, E. Kuhn, B. Segelke, W. Benner, B. Chromy, M. Coleman, G. Bench, P. Hoeprich and T. Sulchek. 2009. Atomic force microscopy differentiates discrete size distributions between membrane protein containing and empty nanolipoprotein particles. BBA - Biomembranes 1788: 724-731. https://doi.org/10.1016/j.bbamem.2008.11.019
9. Blanchette, C., B. Segelke, N. Fischer, M. Corzett, E. Kuhn, J. Cappuccio, W. Benner, M. Coleman, B. Chromy and G. Bench. 2009. Characterization and Purification of Polydisperse Reconstituted Lipoproteins and Nanolipoprotein Particles. International Journal of Molecular Sciences 10: 2958-2971. https://www.mdpi.com/1422-0067/10/7/2958
8. Cappuccio, J., A. Hinz, E. Kuhn, J. Fletcher, E. Arroyo, P. Henderson, C. Blanchette and W. (...). 2009. Cell-free expression for nanolipoprotein particles. Methods in Molecular Biology (Clifton, N.J.).
7. Blanchette, C., R. Law, W. Benner, J. Pesavento, J. Cappuccio, V. Walsworth, E. Kuhn, (...) and T. Sulchek. 2008. Quantifying size distributions of nanolipoprotein particles with single-particle analysis and molecular dynamic simulations. Journal of Lipid Research. https://doi.org/10.1194/jlr.M700586-JLR200
6. COLEMAN, M., P. HOEPRICH, E. ARROYO and J. CAPPUCCIO. 2008. METHODS AND SYSTEMS FOR MONITORING PRODUCTION OF A TARGET PROTEIN IN A NANOLIPOPROTEIN PARTICLE. Patent Cooperation Treaty Application. https://patentscope.wipo.int/search/en/detail.jsf?docId=WO2008141230
5. Cappuccio, J., C. Blanchette, T. Sulchek, E. Arroyo, J. Kralj, A. Hinz, E. Kuhn and B. Chromy. 2008. Cell-free co-expression of functional membrane proteins and apolipoprotein, forming soluble nanolipoprotein particles. Mol Cell Proteomics. 2008 Nov; 7(11): 2246–2253. doi: 10.1074/mcp.M800191-MCP200
4. Katzen, F., J. Fletcher, J. Yang, D. Kang, T. Peterson, J. Cappuccio, C. Blanchette, (...) and W. Kudlicki. 2008. Insertion of membrane proteins into discoidal membranes using a cell-free protein expression approach. J. Proteome Res. 2008, 7, 8, 3535–3542. https://pubs.acs.org/doi/abs/10.1021/pr800265f
3. Chromy, B., E. Arroyo, C. Blanchette, G. Bench, H. Benner, J. Cappuccio, M. Coleman, P. Henderson, A. Hinz and E. Kuhn. 2007. Different Apolipoproteins Impact Nanolipoprotein Particle Formation. Journal of the American Chemical Society 129: 14348-14354. https://pubs.acs.org/doi/abs/10.1021/ja074753y
2. Szundi, I., J. Cappuccio and O. Einarsdóttir. 2004. Amplitude analysis of single-wavelength time-dependent absorption data does not support the conventional sequential mechanism for the reduction of dioxygen to water catalyzed by bovine heart cytochrome c oxidase. Biochemistry 2004, 43, 50, 15746–15758. https://pubs.acs.org/doi/10.1021/bi049408p
1. Cappuccio, J., I. Ayala, G. Elliott, I. Szundi, J. Lewis, J. Konopelski, B. Barry and O. Einarsdottir. 2002. Modeling the active site of cytochrome oxidase. Journal of the American Chemical Society: 1750-1760. https://pubs.acs.org/doi/10.1021/ja011852h
Szundi, I., J. Cappuccio, N. Borovok, A. Kotlyar and O. Einarsdottir. 2001. Photoinduced Electron Transfer in the Cytochrome c/Cytochrome c Oxidase Complex Using... Biochemistry 40: 2186-2193. https://pubs.acs.org/doi/abs/10.1021/bi002341v
