  In this article, we discuss metal-protein interactions in the Ag-lysozyme
complex by spectroscopic measurements. The analysis of the variation in
relative intensities of SERS bands reveal the orientation and the change in
conformation of the protein molecules on the Ag surface with time. The
interaction kinetics of metal-protein complexes has been analyzed over a period
of three hours via both Raman and absorption measurements. Our analysis
indicates that the Ag nanoparticles most likely interact with Trp-123 which is
in close proximity to Phe-34 of the lysozyme molecule.
