Raman Spectroscopy Of Transient Intermediates In Protein-Ligand Binding

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.