Abstract

Formation and characterization of organic thin film assemblies intended for use in biomolecular devices, such as biosensors, is currently a very active area of research. We have been investigating techniques for creating macroscopically ordered protein films formed by covalent bonding between a unique site on the protein and an appropriately derivatized substrate surface. Assemblies consisting of heme proteins immobilized on substrates coated with self-assembled monolayers and Langmuir-Blodgett are being examined. Macroscopic film order is probed using a combination of total internal reflectance fluorescence and planar integrated optical waveguide-attenuated total reflection spectroscopies, from which the orientation distribution of heme tilt angles in the protein film is determined.

© 1997 Optical Society of America