Evidence of conformational changes in adsorbed lysozyme molecule on silver colloids.
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 reveals 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 3h via Raman measurements. Our analysis indicates that the Ag nanoparticles most likely interact with Trp123 which is in close proximity to Phe34 of the lysozyme molecule.
Chandra
Goutam
G
Department of Physics, Indian Institute of Technology, Kharagpur, India.
Ghosh
Kalyan S
KS
Dasgupta
Swagata
S
Roy
Anushree
A
D000327:Adsorption; D000577:Amides / Q000737:chemistry; D000818:Animals; D003102:Colloids; D004220:Disulfides / Q000737:chemistry; D007700:Kinetics; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation / Q000187:drug effects; D012834:Silver / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D013059:Spectrum Analysis, Raman; D014732:Vibration
D000577:Amides; D003102:Colloids; D004220:Disulfides; D012834:Silver; D009113:Muramidase