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Proceedings Paper

Raman Spectroscopy Of Transient Intermediates In Protein-Ligand Binding
Author(s): Warner L. Peticolas; K. Jeff Wilson; B. Mark Britt
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Paper Abstract

Two techniques are described for obtaining the Raman spectra of transient intermediates formed upon the binding of ligands to proteins. In the first of these the far ultraviolet line at 239 nm is used to take the spectrum of a flowing mixture of protein and ligand. In the second technique, the Raman spectra are taken from the interior of an enzyme crystal as substrate diffuses in from the mother liquor and is converted to the product through a series of chemical intermediates. Methods for interpreting the data are discussed.

Paper Details

Date Published: 8 May 1989
PDF: 14 pages
Proc. SPIE 1057, Biomolecular Spectroscopy, (8 May 1989); doi: 10.1117/12.951659
Show Author Affiliations
Warner L. Peticolas, University of Oregon (United States)
K. Jeff Wilson, University of Oregon (United States)
B. Mark Britt, University of Oregon (United States)


Published in SPIE Proceedings Vol. 1057:
Biomolecular Spectroscopy
Robert R. Birge; Henry H. Mantsch, Editor(s)

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