David S Kliger
|Division||Physical & Biological Sciences|
|Department||PBSci-Chemistry & Biochemistry Department|
|Office||Physical Sciences 154|
|Campus Mail Stop||Chemistry|
My research group spans the fields of physical chemistry and biophysics. As physical chemists we have been involved in developing a variety of time-resolved spectroscopic techniques and applying them to a wide range of photochemical, photophysical, and photobiological problems. We have developed perhaps the most sensitive system for measuring nanosecond time-resolved absorption spectra available anywhere as well as analysis techniques to efficiently extract maximum mechanistic information from the data. In addition, we have developed techniques to measure spectra with polarization information which provide more molecular structural information than available from unpolarized absorption spectra. These techniques take advantages of both absorption differences and refractive index differences for polarized light. They can be used to study linear dichroism, with ~100 times more sensitivity than standard techniques used by others, or linear birefringence using linearly polarized light. We have also developed methods to measure circular dichroism, magnetically induced circular dichroism, optical rotatory dispersion, and magnetically induced optical rotatory dispersion using elliptically polarized light. These techniques provide a powerful set of tools for studying molecular dynamic processes. As biophysicists, we apply these tools to study processes important to life. We study the mechanism of activation of visual pigments, the mechanisms of function of the plant regulatory protein phytochrome and a variety of heme proteins, such as myoglobin, hemoglobin, and cytochrome c oxidase, as well as the early events in the folding of a variety of proteins and DNA. Because our experimental capabilities are unmatched in any other laboratory we are frequently asked by people around the world to collaborate on studies of a wide range of systems. This gives us the opportunity to investigate many biological processes with collaborators around the world who are leading experts on each process. We learn a great deal from our collaborators and have fun learning about how biomolecules work.
Biography, Education and Training
B.S., Rutgers University
Ph.D., Cornell University
- I. Szundi, C. Funatogawa and D.S. Kliger, "The Complexity of Bovine Rhodopsin Activation Revealed at Low Temperature and Alkaline pH," Biochemistry 55, 5095 (2016). DOI:10.1021/acs.biochem.6b00687.
- R.M. Esquerra, B.M. Bibi, P. Tipguniakant, I. Birukou, J. Soman, J.S. Olson, D.S. Kliger, and R.A. Goldbeck, "The Role of Heme Pocket Water in Allosteric Regulation of Ligand Reactivity in Human Hemoglobin," Biochemistry 55, 4005 - 4017 (2016). DOI:10.1021/acs.biochem.6b00681.
- I. Szundi, R. Bogomolni, and D.S. Kliger, "Platymonas subcordiformis Channelrhodopsin-2 Function. Part II: Relationship of the Photochemical Reaction Cycle to Channel Currents," J. Biol. Chem. 290, 16585 (2015).
- I. Szundi, H. Li, E.E. Chen, R. Bogomolni, J.L. Spudich, and D.S. Kliger, "Platymonas subcordiformis Channelrhodopsin-2 Function. Part I: The Photochemical Reaction Cycle," J. Biol. Chem. 290, 16573 (2015).
- E. Chen, A. Christiansen, Q. Wang, M.S. Cheung, D.S. Kliger, and P. Wittung-Stafshede. "Effects of Macromolecular Crowding on Burst Phase Kinetics of Cytochrome c Folding," Biochemistry 50, 9836 (2012).
- D.S. Kliger, E. Chen and R.A. Goldbeck, "Probing Kinetic Mechanisms of Protein Function and Folding with Time-Resolved Natural and Magnetic Chiroptical Spectroscopies," International Journal of Molecular Science 13, 683 (2012).
- R.M. Esquerra, I. Lopez-Pena, P. Tipgunlakant, I. Birukou, R-L Nguyen, J. Soman, J.S. Olson, D.S. Kliger, and R.A. Goldbeck, "Kinetic Spectroscopy of Heme Hydration and Ligant Binding in Myoglobin and Isolated Hemoglobin Chains: An Optical Windown into the Functional Dynamics of Water in the Heme Pocket," Phys Chem. Chem. Phys. 12, 10270 (2010).
- E. Chen, R.A. Goldbeck, and D.S. Kliger, "Nanosecond Time-Resolved Polarizations Spectroscopies: Tools for Probing Protein Reaction Mechanisms," Methods 52, 3 (2010).