Picosecond circular dichroism spectroscopy: experiment, theory, and applications to protein dynamics

Sunney Xie; John Douglas Simon

doi:10.1117/12.17688

1 May 1990 Picosecond circular dichroism spectroscopy: experiment, theory, and applications to protein dynamics

Sunney Xie, John Douglas Simon

Proceedings Volume 1204, Time-Resolved Laser Spectroscopy in Biochemistry II; (1990) https://doi.org/10.1117/12.17688
Event: OE/LASE '90, 1990, Los Angeles, CA, United States

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.

Citation Download Citation

Sunney Xie and John Douglas Simon "Picosecond circular dichroism spectroscopy: experiment, theory, and applications to protein dynamics", Proc. SPIE 1204, Time-Resolved Laser Spectroscopy in Biochemistry II, (1 May 1990); https://doi.org/10.1117/12.17688

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