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Chemistry and Biochemistry
University of California
230 Physical Sciences Bldg.
Santa Cruz, CA 95064
Phone: (831) 459-4002
Fax: (831) 459-2935
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David Kliger Professor of Chemistry Executive Vice Chancellor and Provost B.S., Rutgers University Ph.D., Cornell University Office: 154 PSB Phone: (831) 459-2106 Fax: (831) 459-2935 kliger@chemistry.ucsc.edu

Kliger Research Group Department of Chemistry University of California 1156 High Street Santa Cruz, CA 95064 Office Hours Class Times & Locations Labs: 195 PSB, 9-4007

RESEARCH INTERESTS: Physical Chemistry, Biophysics, Time-Resolved Spectroscopy

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.

SELECTED PUBLICATIONS

E.C.Y Yan, J. Epps, J.W. Lewis, I. Szundi, A. Bhagat, T.P. Sakmar, and D.S. Kliger, ìPhotointermediates of the Rhodopsin S186A Mutant as a probe of the Hydrogen Bond Network in the Chromophore Pocket and Counterion Switch,î J. Phys. Chem. C. 111, 8843 (2007).

C.J. Abel, R.A. Goldbeck, R.F. Latypov, H. Roder, and D.S. Kliger, ìConformational Equilibration Time of Unfolded Protein Chains and the Folding Speed Limit,î Biochemistry 46, 4090 (2007).

R.A. Goldbeck, S. Bhaskaran, C. Ortega, J. Mendoza, J.S. Olson, J. Soman, D.S. Kliger, and R.M Esquerra, ìWater and Ligand Entry in Myoglobin: Assessing the Speed and Extent of Heme Pocket Hydration After CO Photodissociation,î Proc. Natl. Acad. Sci. U.S.A. 103, 1254 (2006).

E. Chen, C.E.M. Strauss, Y.Wen, J.W. Lewis, R.A. Goldbeck, and D.S. Kliger, „Nanosecond Laser Temperature-Jump ORD: Application to Early Events in Protein Folding/Unfolding,‰ Rev. Sci. Inst.76, 083120 (2005).

J.W. Lewis, I. Szundi, M.A. Kazmi, T.P. Sakmar, and D.S. Kliger, „Time-Resolved Photointermediate Changes in Rhodopsin Glu181 Mutants,‰ Biochemistry 43,12614 (2004).

R.A. Goldbeck, R.M. Esquerra, D.S. Kliger, J.M. Holt, and G.K. Ackers, „The Molecular Code for Hemoglobin Allostery Revealed by Linking the Thermodynamics and Kinetics of Quaternary Structural Change. 2. Cooperative Free Energies of (áFeCO)2(âCo)2 and (áCo)2(âFeCO)2 T-State Tetramers,‰ Biochemistry 43, 12065 (2004).

R.A. Goldbeck, R.M. Esquerra, J.M. Holt, G.K. Ackers, and D.S. Kliger, „The Molecular Code for Hemoglobin Allostery Revealed by Linking the Thermodynamics and Kinetics of Quaternary Structural Change. I. Microstate Linear Free Energy Relations,‰ Biochemistry 43, 12048 (2004).

E. Chen, R.A. Goldbeck, and D.S. Kliger, „The Earliest Events in Protein Folding: A Structural Requirement for Ultrafast Folding in Cytochrome c,‰ J. Am. Chem. Soc. 126, 11175 (2004).