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Proceedings Paper

Probing protein photochemistry and dynamics with ultrafast infrared spectroscopy
Author(s): Kristen A. Peterson; William H. Woodruff; R. Brian Dyer
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Paper Abstract

Ultra-fast time-resolved infrared spectroscopy is discussed as a tool for investigating protein dynamics. Due to continuing developments in laser technology, researchers have recently begun to take advantage of the utility of vibrational spectroscopies as structural probes in studying the fast timescale dynamics of complex macromolecular systems. The structural complexity of proteins necessitates a wide range of infrared frequencies and timescales in order to obtain a detailed understanding of their conformational dynamics. Free electron lasers are uniquely well suited to this task, as designs are possible which provide ultra-short coherent light pulses throughout the infrared spectral region. Studies planned for the Stanford Picosecond FEL Center on reaction dynamics in the trans-membrane cytochrome oxidase proteins and protein folding in polypeptides are described. These serve as examples of the contributions free electron lasers will make in the fields of biochemistry and biophysics.

Paper Details

Date Published: 14 July 1993
PDF: 5 pages
Proc. SPIE 1854, Free-Electron Laser Spectroscopy in Biology, Medicine, and Materials Science, (14 July 1993); doi: 10.1117/12.148035
Show Author Affiliations
Kristen A. Peterson, Stanford Univ. (United States)
William H. Woodruff, Los Alamos National Lab. (United States)
R. Brian Dyer, Los Alamos National Lab. (United States)

Published in SPIE Proceedings Vol. 1854:
Free-Electron Laser Spectroscopy in Biology, Medicine, and Materials Science
H. Alan Schwettman, Editor(s)

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