Abstract

Self-assembling monolayers are physisorbed on metal mesh as a supporting struture for a protein being analyzed. A protein is embedded into a supported phospholipid bilayer membrane that is stacked between two microarray square-holed meshes of the same metal (either copper or nickel). Fourier transformed infrared (IR) microscopy and spectroscopy was used to observe the molecular vibration of protein dynamic and interaction by measuring the absorption of light that passes through the square holes of the mesh. This phenomenon of the extraordinary optical transmission (EOT) has been observed in the visible and in the IR. An enhanced amount of light is transmitted through the mesh due to propagating surface plasmons that are formed when photons hit and excite the conducting electrons on the surface of the metal creating surface waves. This extra amount of light was used to study the protein interaction structurally and dynamically while embedded within a lipid bilayer membrane. Work with liposomes and extract rabbit powder has been done but not within a bilayer lipid membrane to give an extremely similar example of how the protein actually occurs in vivo. Preliminary results were obtained by observing the interaction of globular actin as it changes to fibrous actin as it begins to form the microtubules of the cytoskeleton. Further studies are being conducted on L-Glutathione, a tripeptide protein residue of the anti-freeze protein. Further studies of the residue will give a good example of the anti-freeze protein dynamics in the membrane and may lead to understanding its role in protecting a cell from becoming cancerous.

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