14 March 2013 Ultrabroadband terahertz spectroscopies of biomolecules and water
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We describe the use of a range of modern spectroscopic techniques—from terahertz time-domain spectroscopy (THz- TDS) to high dynamic-range femtosecond optical Kerr-effect (OKE) spectroscopy—to study the interaction of proteins, peptides, and other biomolecules with the aqueous solvent. Chemical reactivity in proteins requires fast picosecond fluctuations to reach the transition state, to dissipate energy, and (possibly) to reduce the width and height of energy barriers along the reaction coordinate. Such motions are linked with the structure and dynamics of the aqueous solvent making hydration critical to function. These dynamics take place over a huge range of timescales: from the nanosecond timescale of diffusion of water molecules in the first solvation shell of proteins, picosecond motions of amino-acid side chains, and sub-picosecond librational and phonon-like motions of water. It is shown that a large range of frequencies from MHz to THz is accessible directly using OKE resulting in the reduced anisotropic Raman spectrum and by using a combination of techniques including THz-TDS resulting in the dielectric spectrum. Using these techniques, we can now observe very significant differences in the spectra of proteins in aqueous solvent in the 3-30 THz range and more subtle differences at lower frequencies (10 GHz-3 THz).
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David Turton, David Turton, Thomas Harwood, Thomas Harwood, Adrian Lapthorn, Adrian Lapthorn, Elizabeth Ellis, Elizabeth Ellis, Klaas Wynne, Klaas Wynne, "Ultrabroadband terahertz spectroscopies of biomolecules and water", Proc. SPIE 8623, Ultrafast Phenomena and Nanophotonics XVII, 862303 (14 March 2013); doi: 10.1117/12.2003796; https://doi.org/10.1117/12.2003796

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