Evidence of Conformational Changes in Adsorbed Lysozyme Molecule on Silver Colloids

TL;DR

This study investigates how lysozyme proteins change their shape when adsorbed onto silver nanoparticles, using spectroscopic techniques to analyze conformational and orientation changes over time.

Contribution

It provides new insights into the dynamic conformational changes and specific interaction sites of lysozyme on silver colloids through combined spectroscopic analysis.

Findings

Lysozyme undergoes conformational changes upon adsorption to silver nanoparticles.

The interaction primarily involves Trp-123 near Phe-34.

Conformational changes occur over a three-hour period.

Abstract

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.