Publications
- Goldenberg, D. P. (2021). Protein folding and assembly. In Encyclopedia of Biological Chemistry (Jez, J., ed.), 3rd Edition. Elsevier.
Published, 07/2021.
https://www.elsevier.com/books/encyclopedia-of-bio... - King, J. & Goldenberg, D., Goldstein, G., et. al (2021). Congressional budget responses to the pandemic: Fund health care, not warfare. (pp. 200-201). Vol. 111. Am. J. Public Health. Published, 06/2021.
- King, J. & Chal e, M., Chomsky, N., Cirincione, J., Decatur, S., Franklin, M., Goldenberg, D. P., et.al (2020). Uphold the nuclear weapons test moratorium. (pp. 262-262). Vol. 369. Science. Published, 07/2020.
- Goldenberg, D. P. (2015). Principles of NMR spectroscopy: An illustrated guide. University Science Books. An introductory text book on NMR spectroscopy, intended for graduate students, advanced undergraduates and others. ISBN 978-1-891389-88-7. Published, 01/2016.
- Goldenberg, D. P. & Argyle, B. (2014). Minimal effects of macromolecular crowding on an intrinsically disordered protein: A small-angle neutron scattering study. Biophys. J., 106, 905–914. http://dx.doi.org/10.1016/j.bpj.2013.12.003.
Published, 02/2014.
http://dx.doi.org/10.1016/j.bpj.2013.12.003 - Goldenberg, D. P. & Argyle, B. (2014). Self crowding of globular proteins studied by small-angle X-ray scattering. Biophys. J., 106, 895–904. http://dx.doi.org/10.1016/j.bpj.2013.12.004.
Published, 02/2014.
http://dx.doi.org/10.1016/j.bpj.2013.12.004 - [Goldenberg, D. P. (2013). Protein folding and assembly. In Encyclopedia of Biological Chemistry (Lennarz, W. J. & Lane, M., eds.), volume 3, pp. 625–631. Academic Press, Waltham, MA, 2nd edition. http://dx.doi.org/10.1016/B978-0-12-378630-2.00064-5.
Published, 01/2013.
http://dx.doi.org/10.1016/B978-0-12-378630-2.00064... - Johansen, D., Jeffries, C. M. J., Hammouda, B., Trewhella, J. & Goldenberg, D. P. (2011). Effects of macromolecular crowding on an intrinsically disordered protein characterized by small-angle neutron scattering with contrast matching. Biophys. J., 100, 1120–1128.
Published, 02/2011.
http://dx.doi.org/10.1016/j.bpj.2011.01.020 - Zakharova, E., Horvath, M. P. & Goldenberg, D. P. (2009). Structure of a serine protease poised to resynthesize a peptide bond. Proc. Natl. Acad. Sci., USA, 106, 11034–11039.
Published, 07/2009.
http://dx.doi.org/10.1073/pnas.0902463106 - Zakharova, E., Horvath, M. P. & Goldenberg, D. P. (2008). Functional and structural roles of the Cys14-Cys38 Disulfide of Bovine Pancreatic Trypsin Inhibitor. J. Mol. Biol., 382, 998–1013.
Published, 10/2008.
http://dx.doi.org/10.1016/j.jmb.2008.07.063 - Wang, Y., Trewhella, J. & Goldenberg, D. P. (2008). Small-angle x-ray scattering of reduced ribonuclease A: Effects of solution conditions and comparisons with a computational model of unfolded proteins. J. Mol. Biol., 377, 1576–1592.
Published, 04/2008.
http://dx.doi.org/10.1016/j.jmb.2008.02.009 - Hanson, W. M., Domek, G. J., Horvath, M. P. & Goldenberg, D. P. (2007). Rigidification of a flexible protease inhibitor variant upon binding to trypsin. J. Mol. Biol., 366, 230–243.
Published, 02/2007.
http://dx.doi.org/10.1016/j.jmb.2006.11.003
Research Statement
The long-range goal of my research is to understand the role of protein dynamics in determining the stabilities of protein structures, the specificity of their formation and their functional properties. Our current efforts are focused on two aspects of protein dynamics. The first is the characterization of unfolded proteins, which are now recognized to play important roles in vivo. We are particularly interested in determining how the properties of unfolded proteins change in response to solution conditions and the presence of high concentrations of other macromolecules, as found intracellularly. The second focus of our work is the interaction between a protease, trypsin, and a natural inhibitor of this enzyme, bovine pancreatic trypsin inhibitor (BPTI). BPTI is a member of a large class of natural protease inhibitors that act by binding to the active sites of their targets, much as a substrate would, but are resistant to hydrolysis. We believe that the rigidity of the enzyme-inhibitor complex is key to preventing the catalytic reaction, and we are currently using NMR spectroscopy, thermodynamic and kinetic measurements and x-ray crystallography to learn more about the factors that determine flexibility in the context of an enzyme-substrate complex and about the nature of the motions that are necessary for catalytic function.
Research Keywords
- Protein Structure
- Protein Folding
- NMR Spectroscopy
Presentations
- Telluride Workshop on Macromolecular Crowding, Telluride, CO. Invited Talk/Keynote, Presented, 06/2015.
- Telluride Workshop on Macromolecular Crowding, Telluride, CO. Invited Talk/Keynote, Presented, 06/01/2013.
- Telluride Workshop on Macromolecular Crowding, Telluride, CO. Invited Talk/Keynote, Presented, 06/2011.
Research Groups
- Timothy Luger, Undergraduate Student. 05/2012 - 05/2014.
- Sabrina Aderibigbe, Undergraduate Student. Biology. 05/2012 - 05/2013.
- Gourab Bhattacharje, Graduate Student. Biology. 05/2011 - 05/2014.
- Brian Argyle, Technician. Biology. 05/2011 - 01/2013.
- Chae Kyung Yoo, Undergraduate Student. Biology. 05/2010 - 05/2014.
Software Titles
- Utah SAXS Tools. A suite of programs for processing and analyzing small-angle X-ray and neutron scattering data. Available for download from: http://bioweb.biology.utah.edu/goldenberg/software.shtml. Release Date: 05/2012. Inventors: David P. Goldenberg.
- MaSpec II. A Macintosh program for controlling and collecting data from UV-visible spectrophotometers via a serial port connection. http://bioweb.biology.utah.edu/goldenberg/software.shtml Most recently updated, December 2014 . Release Date: 01/2000. Inventors: Benjamin P. Goldenberg and David P. Goldenberg.
Languages
- English, fluent.