Abstract
Pulsed THz spectroscopy provides a new method for probing the tertiary structure and hydration of biomolecules. In proteomics applications, the response of a protein-protein structure must be probed quickly and non-invasively. THz-frequency radiation lies in the far infrared, a region associated with structural motion modes of large molecules. The THz region has been difficult to probe in the past with Fourier Transform Infrared (FTIR) techniques, but recently the advent of pulsed THz spectroscopy (PTS) has enabled the study of molecular denaturation and hydration.1 We a.re interested in using PTS to charac-terize the conformation and hydration of enzymatic proteins for biochip analysis.
© 2002 Optical Society of America
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