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Updated: May 30, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Protein conformational changes revealed by optical spectroscopic reflectometry in porous silicon multilayers
Edoardo De Tommasi1, Ilaria Rea, Ivo Rendina
1National Council of Research, Institute for Microelectronic and Microsystems, Department of Naples, Via P Castellino 111, I-80131 Naples, Italy.
Abstract:
The protein-ligand molecular interactions imply strong geometrical and structural rearrangements of the biological complex which are normally detected by high sensitivity optical techniques such as time-resolved fluorescence microscopy. In this work, we have measured, by optical spectroscopic reflectometry in the visible-near-infrared region, the interaction between a sugar binding protein (SBP), covalently bound on the surface of a porous silicon (PSi) microcavity, and glucose, at different concentrations and temperatures. Variable-angle spectroscopic ellipsometric (VASE) characterization of protein-functionalized PSi layers confirms that the protein-ligand system has an overall volume smaller than the SBP alone.
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