Abstract
We measured ultrafast structural relaxations in horse carboxymyoglobin (MbCO) using heterodyne-detected transient grating spectroscopy. The anisotropic component of the protein response to photodissociation was isolated by acquiring all nonzero elements of the complex third-order nonlinear susceptibility (X (3)) tensor.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
L. Genburg et al., Science 251, 1051 (1991).
G. Daduse, G.D. Goodno, H.L. Chili, J. Ogilvie, and R.J.D. Miller, sub. for publ.
G.D. Goodno, G. Dadusc, and R.J.D. Miller, J. Opt. Soc. Am. B 15, 1791 (1998).
R. W. Hellwarth, Prog. Quant. Eleetr. 5, 1 (1977).
A. Ansari et al., Biophys. J. 64, 852 (1993).
J. Deak, H.L. Chiu, C. Lewis, and R.J.D. Miller, J. Phys. Chem. (in press) (1998).
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1998 Springer-Verlag Berlin Heidelberg
About this paper
Cite this paper
Goodno, G.D., Astinov, V., Miller, R.J.D. (1998). Characterization of the Complex Third-order Susceptibility of Myoglobin using Diffractive Optics. In: Ultrafast Phenomena XI. Springer Series in Chemical Physics, vol 63. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-72289-9_40
Download citation
DOI: https://doi.org/10.1007/978-3-642-72289-9_40
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-72291-2
Online ISBN: 978-3-642-72289-9
eBook Packages: Springer Book Archive