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Proceedings Paper

Using terahertz spectroscopy as a protein binding assay
Author(s): Jing-Yin Chen; Joseph R. Knab; Shuji Ye; Yunfen He; Andrea G. Markelz
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Paper Abstract

The vibrational modes corresponding to protein tertiary structural motion lay in the far infrared or terahertz frequency range. These collective large scale motions depend on global structure and thus will necessarily be perturbed by ligand binding events. We discuss the use of terahertz dielectric spectroscopy to measure these vibrational modes and the sensitivity of the technique to changes in protein conformation, oxidation state and environment. A challenge of applying this sensitivity as a spectroscopic assay for ligand binding is the sensitivity of the technique to both bulk water and water bound to the protein. This sensitivity can entirely obscure the signal from the protein or protein-ligand complex itself, thus necessitating sophisticated sample preparation making the technique impractical for industrial applications. We discuss methods to overcome this background and demonstrate how terahertz spectroscopy can be used to quickly assay protein binding for proteomics and pharmaceutical research.

Paper Details

Date Published: 25 February 2006
PDF: 8 pages
Proc. SPIE 6080, Advanced Biomedical and Clinical Diagnostic Systems IV, 608006 (25 February 2006); doi: 10.1117/12.664098
Show Author Affiliations
Jing-Yin Chen, SUNY/Buffalo (United States)
Joseph R. Knab, SUNY/Buffalo (United States)
Shuji Ye, SUNY/Buffalo (United States)
Yunfen He, SUNY/Buffalo (United States)
Andrea G. Markelz, SUNY/Buffalo (United States)


Published in SPIE Proceedings Vol. 6080:
Advanced Biomedical and Clinical Diagnostic Systems IV
Gerald E. Cohn; Warren S. Grundfest; David A. Benaron; Tuan Vo-Dinh, Editor(s)

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