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Proceedings Paper

Ultrafast nonlinear optical studies of protein dynamics
Author(s): Lynn Schilling; Stephen P. Palese; R. J. Dwayne Miller
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Paper 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.

Paper Details

Date Published: 17 June 1993
PDF: 5 pages
Proc. SPIE 1921, Laser Spectroscopy of Biomolecules, (17 June 1993); doi: 10.1117/12.146124
Show Author Affiliations
Lynn Schilling, Univ. of Rochester (United States)
Stephen P. Palese, Univ. of Rochester (United States)
R. J. Dwayne Miller, Univ. of Rochester (Canada)


Published in SPIE Proceedings Vol. 1921:
Laser Spectroscopy of Biomolecules

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