Megan Thielges, Stanford University, "Nonlinear Spectroscopy, Protein Dynamics, and Biological Molecular Recognition"
Tuesday, December 6, 2011
"Nonlinear Spectroscopy, Protein Dynamics, and Biological Molecular Recognition" Abstract: Protein motions on a broad range of timescales impact protein function. I will describe how nonlinear spectroscopy can be employed to study fast protein motions and their potential involvement in biological molecular recognition. In one example, visible three photon echo spectroscopy was used to characterize the dynamic diversity within the antibody response to a chromophoric antigen. I will then discuss the application of two dimensional infrared (2D IR) spectroscopy to characterize the dynamics of the enzyme cytochrome P450cam and their potential contribution to the specificity of molecular recognition. Finally, I will describe my recent efforts to generalize the application of 2D IR spectroscopy to study dynamics throughout any protein by combining 2D IR spectroscopy with the site-specific incorporation of amino acids bearing vibrational probes.