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Proceedings Paper

Picosecond circular dichroism spectroscopy: experiment, theory, and applications to protein dynamics
Author(s): Sunney Xie; John Douglas Simon
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Paper Abstract

An experimental technique for measuring time dependent circular dichroism signals with picosecond resolution is described. The details of the experimental apparatus are presented. Theoretical modeling of the detected signal demonstrates that the circular dichroism signal can be isolated from contributions due to pump-induced linear dichroism and linear birefringence effects. The experimental apparatus is used to examine the comformation relaxation in myoglobin following the photoelimination of CO from carbonmonoxymyoglobin. Probing the circular dichroism of the N-band of the herne at 355 nm reveals a relaxation of several hundreds of picosecond, over two orders of magnitude slower than the photo-induced bond cleavage. These results are discussed in terms of the restructuring of the protein following photodissociation.

Paper Details

Date Published: 1 May 1990
PDF: 12 pages
Proc. SPIE 1204, Time-Resolved Laser Spectroscopy in Biochemistry II, (1 May 1990); doi: 10.1117/12.17688
Show Author Affiliations
Sunney Xie, Univ. of California/San Diego (United States)
John Douglas Simon, Univ. of California/San Diego (United States)


Published in SPIE Proceedings Vol. 1204:
Time-Resolved Laser Spectroscopy in Biochemistry II
Joseph R. Lakowicz, Editor(s)

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