No data available.
Please log in to see this content.
You have no subscription access to this content.
No metrics data to plot.
The attempt to load metrics for this article has failed.
The attempt to plot a graph for these metrics has failed.
The full text of this article is not currently available.
Sub-terahertz spectroscopy reveals that proteins influence the properties
of water at greater distances than previously detected
1.M. Chaplin, “Opinion: Do we underestimate the importance of water in cell biology?,” Nat. Rev. Mol. Cell Biol. 7, 861–866 (2006).
2.T. H. Basey-Fisher, S. M. Hanham, H. Andresen, S. A. Maier, M. M. Stevens, N. M. Alford, and N. Klein, “Microwave Debye relaxation analysis of dissolved proteins: Towards free-solution biosensing,” Appl. Phys. Lett. 99, 233703 (2011).
3.S. C. Saha, J. P. Grant, Y. Ma, A. Khalid, F. Hong, and D. R. S. Cumming, “Application of terahertz spectroscopy to the characterization of biological samples using birefringence silicon grating,” J. Biomed. Opt. 17(6), 067006 (2012).
4.S. Laurette, A. Treizebre, F. Affouard, and B. Bocquet, “Subterahertz characterization of ethanol hydration layers by bicrofluidic system,” Appl. Phys. Lett. 97, 111904 (2010).
5.D. M. Leitner, M. Gruebele, and M. Havenith, “Solvation dynamics of biomolecules: Modeling and terahertz experiments,” HFSP J. 2, 314–323 (2008).
7.A. G. Markelz, A. Roitberg, and E. J. Heilweil, “Pulsed terahertz spectroscopy of DNA, bovine serum albumin and collagen between 0.1 and 2.0 THz,” Chem. Phys. Lett. 320, 42–48 (2000).
8.S. E. Whitmire, D. Wolpert, A. G. Markelz, J. R. Hillebrecht, J. Galan, and R. R. Birge, “Protein flexibility and conformational state: A comparison of collective vibrational modes of wild-type and D96N bacteriorhodopsin,” Biophys. J. 85, 1269–1277 (2003).
10.T. Q. Luong, P. K. Verma, R. K. Mitra, and M. Havenith, “Do hydration dynamics follow the structural perturbation during thermal denaturation of a protein: A terahertz absorption study,” Biophys. J. 101, 925–933 (2011).
11.S. Ebbinghaus, S. J. Kim, M. Heyden, X. Yu, U. Heugen, M. Gruebele, D. M. Leitner, and M. Havenith, “An extended dynamical hydration shell around proteins,” PNAS 104, 20749–20752 (2007).
12.V. Matvejev, Y. Zhang, and J. Stiens, “High performance integrated terahertz sensor for detection of biomolecular processes in solution,” IET Microwaves, Antennas and Propagation 8, 394-400 (2013).
13.J.-Y. Chen, J. R. Knab, S. Ye, Y. He, and A. G. Markelz, “Terahertz dielectric assay of solution phase protein binding,” Appl. Phys. Lett. 90, 243901-1–243901-3 (2007).
17.O. Kambara and K. Tominaga, “Structural fluctuation of proteins revealed by terahertz time-domain spectroscopy,” Spectroscopy 24, 149–152 (2010).
18.N. Q. Vinh, S. J. Allen, and K. W. Plaxco, “Dielectric spectroscopy of proteins as a quantitative experimental test of computational models of their low-frequency harmonic motions,” J. Am. Chem. Soc. 133, 8942–8947 (2011).
19.N. Yamamoto, O. Kambara, K. Yamamoto, A. Tamura, S. Saito, and K. Tominaga, “Temperature and hydration dependence of Low-frequency spectra of poly-L-glutamic acid with different secondary structures studied by terahertz time-domain spectroscopy,” Soft Matter 8, 1997–2006 (2012).
21.S. Laurette, A. Treizebre, A. Elagli, B. Hatirnaz, R. Froidevaux, F. Affouard, L. Duponchel, and B. Bocquet, “Highly sensitive terahertz spectroscopy in microsystem,” RSC Adv. 2, 10064–10071 (2012).
23.S. Gekle and R. R. Netz, “Anisotropy in the dielectric spectrum of hydration water and its relation to water dynamics,” J. Chem. Phys. 137, 104704 (2012).
24.P. U. Jepsen, D. G. Cooke, and M. Koch, “Terahertz spectroscopy and imaging—Modern techniques and applications,” Laser Photonics Rev. 5, 124–166 (2011).
26.T. Ding, R. Li, J. A. Zeitler, T. L. Huber, L. F. Gladden, A. P. J. Middelberg, and R. J. Falconer, “Terahertz and far infrared spectroscopy of alanine-rich peptides having variable ellipticity,” Opt. Express 18, 27431–27444 (2010).
27.P. Glancy and W. P. Beyermann, “Dielectric properties of fully hydrated nucleotides in the terahertz frequency range,” J. Chem. Phys. 132, 245102 (2010).
28.S. Ebbinghaus, K. Meister, B. Born, A. L. De Vries, M. Gruebele, and M. Havenith, “Antifreeze glycoprotein activity correlates with long-range protein-water dynamics,” J. Am. Chem. Soc. 132, 12210–12211 (2010).
29.S. Ebbinghaus, S. J. Kim, M. Heyden, X. Yu, M. Gruebele, D. M. Leitner, and M. Havenith, “Protein sequence- and pH-dependent hydration probed by terahertz spectroscopy,” J. Am. Chem. Soc. 130, 2374–2375 (2008).
30.G. Niehues, M. Heyden, D. A. Schmidt, and M. Havenith, “Exploring hydrophobicity by THz absorption spectroscopy of solvated amino acids,” Faraday Discuss. 150, 193–207 (2011).
31.M. Heyden, E. Bründermann, U. Heugen, G. Niehues, D. M. Leitner, and M. Havenith, “Long-range influence of carbohydrates on the solvation dynamics of waters answers from terahertz absorption measurements and molecular modeling simulations,” J. Am. Chem. Soc. 130, 5773–5779 (2008).
32.T. Arikawa, M. Nagai, and K. Tanaka, “Characterizing hydration state in solution using terahertz time-domain attenuated total reflection spectroscopy,” Chem. Phys. Lett. 457, 12–17 (2008).
33.T. Ding, T. Huber, A. P. J. Middelberg, and R. J. Falconer, “Characterization of low-frequency modes in aqueous peptides using far-infrared spectroscopy and molecular dynamics simulation,” J. Phys. Chem. A 115, 11559–11565 (2011).
34.P. A. George, W. Hui, F. Rana, B. G. Hawkins, A. E. Smith, and B. J. Kirby, “Microfluidic devices for terahertz spectroscopy of biomolecules,” Opt. Express 16, 1577-1582 (2008).
35.H. Yada, M. Nagai, and K. Tanaka, “Origin of the fast relaxation component of water and heavy water revealed by terahertz time-domain attenuated total reflection spectroscopy,” Chem. Phys. Lett. 464, 166–170 (2008).
36.O. Sushko, K. Shala, R. Dubrovka, and R. S. Donnan, “Revised metrology for enhanced accuracy in complex optical constant determination by THz time-domain spectroscopy,” J. Opt. Soc. Am. A 30, 979–986 (2013).
37.L. Duvillaret, F. Garet, and J.-L. Coutaz, “Highly precise determination of optical constants and sample thickness in terahertz time-domain spectroscopy,” Appl. Opt. 38, 409–415 (1999).
39.O. Sushko, R. Dubrovka, and R. S. Donnan, “Terahertz spectral domain computational analysis of hydration shell of proteins with increasingly complex tertiary structure,” J. Phys. Chem. B 117, 16486–16492 (2013).
40.B. Yang, R. J. Wylde, D. H. Martin, P. Goy, R. S. Donnan, and S. Caroopen, “Determination of the gyrotropic characteristics of hexaferrite ceramics from 75 to 600 GHz,” IEEE Trans. Microwave Theory Tech. 58, 3587-3597 (2010).
41.J. W. Bye, S. Meliga, D. Ferachou, G. Cinque, J. A. Zeitler, and R. J. Falconer, “Analysis of the hydration water around bovine serum albumin using terahertz coherent synchrotron radiation,” J. Phys. Chem. A 118, 83–88 (2014).
42.U. Heugen, G. Schwaab, E. Brundermann, M. Heyden, X. Yu, D. M. Leitner, and M. Havenith, “Solute-induced retardation of water dynamics probed directly by terahertz spectroscopy,” PNAS 103, 12301–12306 (2006).
43.J. Xu, K. W. Plaxco, and S. J. Allen, “Probing the collective vibrational dynamics of a protein in liquid water by terahertz absorption spectroscopy,” Protein Sci. 15, 1175–1181 (2006).
44.C. Zhang and S. M. Durbin, “Hydration-induced far-infrared absorption increase in myoglobin,” J. Phys. Chem. B 110, 23607-23613 (2006).
45.B. Born, H. Weingärtner, E. Bründermann, and M. Havenith, “Solvation dynamics of model peptides probed by terahertz spectroscopy. Observation of the onset of collective network motions,” J. Am. Chem. Soc. 131, 3752–3755 (2009).
46.N. Kaun, J. R. Baena, D. Newnham, and B. Lendl, “Terahertz pulsed spectroscopy as a new tool for measuring the structuring effect of solutes on water,” Appl. Spectrosc. 59, 505-510 (2005).
48.J. Qvist, E. Persson, C. Mattea, and B. Halle, “Time scales of water dynamics at biological interfaces: Peptides, proteins and cells,” Faraday Discuss. 141, 131–144 (2009).
49.D. I. Svergun, S. Richard, M. H. J. Koch, Z. Sayers, S. Kuprin, and G. Zaccai, “Protein hydration in solution: Experimental observation by X-ray and neutron scattering,” Proc. Natl. Acad. Sci. U. S. A. 95, 2267–2272 (1998).
50.H. Frohlich, “The extraordinary dielectric properties of biological materials and the action of enzymes,” Proc. Natl. Acad. Sci. U. S. A. 72, 4211–4215 (1975).
51.A. Pertsemlidis, A. M. Saxena, A. K. Soper, T. Head-Gordon, and R. M. Glaeser, “Direct evidence for modified solvent structure within the hydration shell of a hydrophobic amino acid,” Proc. Natl. Acad. Sci. U. S. A. 93, 10769–10774 (1996).
52.M. Harel, G. L. Kleywegt, R. B. Ravelli, I. Silman, and J. L. Sussman, “Crystal structure of an acetylcholinesterase-Fasciculin complex: Interaction of a three-fingered toxin from snake venom with its target,” Structure 3, 1355–1366 (1995).
53.P. Marchot, R. B. G. Ravelli, M. L. Raves, Y. Bourne, D. C. Vellom, J. Kanter, S. Camp, J. L. Sussman, and P. Taylor, “Soluble monomeric acetylcholinesterase from mouse: Expression, purification, and crystallization in complex with Fasciculin,” Protein Sci. 5, 672–679 (1996).
54.D. R. Ripoll, C. H. Faerman, P. H. Axelsen, I. Silman, and J. L. Sussman, “An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase,” Proc. Natl Acad. Sci. U. S. A. 90, 5128–5132 (1993).
55.C. E. Felder, J. Prilusky, I. Silman, and J. L. Sussman, “A Server and database for dipole moments of proteins,” Nucleic Acids Res. 35, W512–W521 (2007).
57.S. Perticaroli, L. Comez, M. Paolantoni, P. Sassi, L. Lupi, D. Fioretto, A. Paciaroni, and A. Morresi, “Broadband depolarized light scattering study of diluted protein aqueous solutions,” J. Phys. Chem. B 114, 8262-8269 (2010).
58.J. Sun, G. Niehues, H. Forbert, D. Decka, G. Schwaab, D. Marx, and M. Havenith, “Understanding THz spectra of aqueous solutions: Glycine in light and heavy water,” J. Am. Chem. Soc. 136, 5031-5038 (2014).
59.R. Li, C. D’Agostino, J. McGregor, M. D. Mantle, A. J. Zeitler, and L. F. Gladden, “Mesoscopic structuring and dynamics of alcohol/water solutions probed by terahertz time-domain spectroscopy and pulsed field gradient nuclear magnetic resonance,” J. Phys. Chem. B 118, 10156-10166 (2014).
60.K.-J. Tielrooij, J. Hunger, R. Buchner, M. Bonn, and H. J. Bakker, “Influence of concentration and temperature on the dynamics of water in the hydrophobic hydration shell of tetramethylurea,” J. Am. Chem. Soc. 132, 15671–15678 (2010).
Article metrics loading...
The initial purpose of the study is to systematically investigate the solvation
properties of different proteins in water solution by terahertz (THz) radiation
absorption. Transmission measurements of protein water solutions
have been performed using a vector network analyser-driven quasi-optical bench
covering the WR-3 waveguide band (0.220–0.325 THz). The following proteins, ranging from
low to high molecular weight, were chosen for this study: lysozyme, myoglobin, and
bovine serum albumin (BSA). Absorption properties of solutions were
studied at different concentrations of proteins ranging from 2 to 100 mg/ml. The
concentration-dependent absorption of protein molecules was
determined by treating the solution as a two-component model first; then, based on
absorptivity, the extent of the hydration shell is estimated. Protein molecules are
shown to possess a concentration-dependent absorptivity in water solutions.
Absorption curves of all three proteins sharply peak
towards a dilution-limit that is attributed to the enhanced flexibility of
and amino acid side chains. An alternative approach to the determination of
hydration shell thickness is thereby suggested, based on protein absorptivity. The
proposed approach is independent of the absorption of the hydration shell. The derived
estimate of hydration shell thickness for each protein supports previous
findings that protein-water interaction dynamics extends beyond
2-3 water solvation-layers as predicted by molecular dynamics simulations and other techniques
such as NMR, X-ray scattering, and neutron scattering. According to our estimations,
the radius of the dynamic hydration shell is 16, 19, and 25 Å, respectively, for
lysozyme, myoglobin, and BSA proteins and correlates with the dipole moment of the
It is also seen that THz
radiation can serve as an initial estimate of the protein
Full text loading...
Most read this month