Ultrafast nonlinear optical studies of protein dynamics

Lynn Schilling; Stephen P. Palese; R. J. Dwayne Miller

doi:10.1117/12.146124

17 June 1993 Ultrafast nonlinear optical studies of protein dynamics

Lynn Schilling, Stephen P. Palese, R. J. Dwayne Miller

Proceedings Volume 1921, Laser Spectroscopy of Biomolecules; (1993) https://doi.org/10.1117/12.146124
Event: Laser Spectroscopy of Biomolecules: 4th International Conference on Laser Applications in Life Sciences, 1992, Jyvaskyla, Finland

Abstract

Optical Kerr effect (OKE) studies of myoglobin and water at wavelength of 627 nanometers with 45 femtosecond pulses have been performed. The nonresonant response of water consists of electronic, translational, librational and relaxational components. The low frequency components observed in the water OKE study are in qualitative agreement with previous depolarized light scattering (DLS) studies and molecular dynamics (MD) simulations. Operation on the edge of the Q-band of the myoglobin resulted in the pulse broadening to 100 fs. Two relaxational components, 195 fs and 2.4 +/- .2 ps were observed in both the carboxy and deoxy myoglobin samples studied. The 195 fs component is assigned to the OKE response of water while the 2.4 ps component is related to the transient birefringence of the myoglobin. A discussion of the origin of the transient signal as well as the calculation leading to the assignment to birefringence as opposed to dichroism is included. With this interpretation, the observed dynamics are related to the low frequency modes of the protein. Information on these modes is needed to understand the initial events that direct functionally important structural changes.

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Lynn Schilling, Stephen P. Palese, and R. J. Dwayne Miller "Ultrafast nonlinear optical studies of protein dynamics", Proc. SPIE 1921, Laser Spectroscopy of Biomolecules, (17 June 1993); https://doi.org/10.1117/12.146124

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