Ultrabroadband terahertz spectroscopies of biomolecules and water

David Turton, Thomas Harwood, Adrian Lapthorn, Elizabeth Ellis, Klaas Wynne

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


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)
Original languageEnglish
Article number862303
JournalProceedings of SPIE: The International Society for Optical Engineering
Publication statusPublished - 14 Mar 2013


  • chemicals
  • diffusion
  • Kerr effect
  • molecules
  • phonons
  • spectroscopy
  • terahertz radiation
  • water


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