Many of the functionally relevant collective vibrations of proteins and other biopolymers are expected to occur at terahertz frequencies. Precise absorption measurements combined with careful titration of biopolymers in water have allowed us to directly measure the terahertz absorption spectra associated with these motions, despite the strong background absorption of the solvent. We have also explored the circular dichroism spectroscopy of biomolecules over this same frequency range. Since circular dichroism requires the presence of net chirality in a molecule and chirality is present in nearly all biomaterial, it has the potential to capture the background free spectral features in biopolymers. To undertake these studies we have developed a broad band terahertz spectrometer suitable for both direct absorption and circular dichroism measurements of proteins in water between 0.75 – 3.72 THz. Direct terahertz absorption spectra of prototypical proteins bovine serum albumin (BSA) and hen egg white lysozyme have been documented and are described here. We have also successfully demonstrated the magnetic circular dichroism in semiconductors, and placed an upper bound on the terahertz circular dichroism signature of solvated BSA. In the terahertz frequency range, it appears that circular dichroism signatures are exceedingly small and detection remains a challenge.
Robust numerical evaluation of circular dichroism from chiral medium/nanostructure coupled systems using the finite-element method
