Abstract
| Language | English |
|---|---|
| Article number | 862303 |
| Journal | Proceedings of SPIE: The International Society for Optical Engineering |
| Volume | 8623 |
| DOIs | |
| Publication status | Published - 14 Mar 2013 |
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Keywords
- chemicals
- diffusion
- Kerr effect
- molecules
- phonons
- spectroscopy
- terahertz radiation
- water
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Ultrabroadband terahertz spectroscopies of biomolecules and water. / Turton, David; Harwood, Thomas; Lapthorn, Adrian; Ellis, Elizabeth; Wynne, Klaas.
In: Proceedings of SPIE: The International Society for Optical Engineering, Vol. 8623, 862303, 14.03.2013.Research output: Contribution to journal › Article
TY - JOUR
T1 - Ultrabroadband terahertz spectroscopies of biomolecules and water
AU - Turton, David
AU - Harwood, Thomas
AU - Lapthorn, Adrian
AU - Ellis, Elizabeth
AU - Wynne, Klaas
PY - 2013/3/14
Y1 - 2013/3/14
N2 - 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)
AB - 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)
KW - chemicals
KW - diffusion
KW - Kerr effect
KW - molecules
KW - phonons
KW - spectroscopy
KW - terahertz radiation
KW - water
UR - http://www.scopus.com/inward/record.url?scp=84878205796&partnerID=8YFLogxK
U2 - 10.1117/12.2003796
DO - 10.1117/12.2003796
M3 - Article
VL - 8623
JO - Proceedings of SPIE
T2 - Proceedings of SPIE
JF - Proceedings of SPIE
SN - 0277-786X
M1 - 862303
ER -