UofM Biophysics Faculty and Staff
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Jennifer P Ogilvie

Assistant Professor of Physics

Jennifer P. Ogilvie
Jennifer P. Ogilvie

Assistant Research Scientist, Biophysics Research Division

PhD: University of Toronto, Canada, 2003

Dept:  Department of Physics
Office Address:  4210 Randall
Phone:  615-0485

Email:  jogilvie@umich.edu



Ogilvie Group Home Page
Our research combines the tools of ultrafast and single molecule spectroscopy and nonlinear microscopy to explore the diverse length and time scales of biology: from single molecules to single organisms, on time scales of femtoseconds, to seconds.

The fastest processes in biology occur within femtoseconds. On this time scale bonds are made and broken, and the motions that ultimately lead to protein function begin. To follow dynamics this fast we need a camera that won’t miss out on the action: that means we need femtosecond time resolution. Ultrafast lasers, which can now be used to generate sub-femtosecond pulses, provide us with the tools we need to access this quantum mechanical realm. Using the versatile tools of ultrafast nonlinear spectroscopy we initiate and probe fundamental processes such as energy and charge transfer that are the engines of biology.

Experimental detection methods are now sensitive enough that we can study biological molecules one at a time. Single molecule spectroscopy provides fundamentally new information that is often buried in an ensemble-averaged measurement. In addition, it is a unique tool for exploring processes that are difficult to synchronize in ensembles, but that are fundamental to biological function, such as protein-protein interactions.

Beyond the length scale of protein-protein interactions lies another order of complexity altogether, where proteins work together to orchestrate cellular processes. Today’s microscopes usually use artificial labels to identify and follow particular molecular species. As an alternative, we can use physical properties of the molecules themselves to reveal their role in cellular function. By bringing the tools of nonlinear spectroscopy to the microscope, we obviate the need for labeling and tap into rich and novel modes of molecular contrast.

Please see our group webpage for further details!
Group Home Page: http://www-personal.umich.edu/~jogilvie/


Representative Publications

J. P. Ogilvie, E. Beaurepaire, A. Alexandrou, M. Joffre, Fourier transform coherent anti-Stokes Raman scattering microscopy, Optics Letters, (2006) 31, 4, 480-482.

J. P. Ogilvie, D. Débarre, X. Solinas, J.-L. Martin, E. Beaurepaire, M. Joffre, Use of coherent control for selective two-photon fluorescence microscopy in live organisms, Optics Express, (2006) #9987.

J. P. Ogilvie, K. Kubarych, A. Alexandrou, M. Joffre, Fourier transform measurement of two-photon excitation spectra: applications to microscopy and optimal control, Optics Letters, (2005) 30, 911-913.

T. Polack, J. P. Ogilvie, S. Franzen, M. Vos, M. Joffre, J.-L. Martin, A. Alexandrou, CO vibration as a probe of ligand dissociation and transfer in myoglobin, Physical Review Letters, (2004) 93, 018102.

M. Cowan, J. P. Ogilvie, R. J. D. Miller, Two-dimensional spectroscopy using diffractive optics based phase-locked photon echoes, Chemical Physics Letters, (2004) 36, 184-189.

M. Armstrong, J. P. Ogilvie, M. Cowan, A. Nagy and R. J. D. Miller, Observation of the Cascaded Atomic to Global Length Scales Driving Protein Motion, Proceedings of the National Academy of Sciences USA, (2003) 100, 4990-4994.

J. P. Ogilvie, M. Plazanet, G. Dadusc and R. J. D. Miller, The dynamics of ligand escape in MbCO: Q-band transient absorption and four-wave mixing studies, Journal of Physical Chemistry B, (2002) 106 10460-10467.

G. Dadusc, J. Ogilvie, P. Schulenberg, U. Marvet, R.J.D. Miller, Diffractive optics-based heterodyne detected four-wave mixing signals of protein motion: from “proteinquakes” to ligand escape in myoglobin, Proceedings of the National Academy of Sciences USA, (2001) 98, 6116-6120.


      
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Last Updated: 5/4/2006
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