Abstract

Terahertz spectra of four alanine-rich peptides with known secondary structures were studied by terahertz time domain spectroscopy (THz-TDS) and by Fourier transform infrared spectroscopy (FTIR) using a synchrotron light source and a liquid-helium cooled bolometer. At ambient temperatures the usable bandwidth was restricted to 0.2-1.5 THz by the absorbance of water. The existence of a solvation shell around the peptide in solution was observed and its size estimated to be between 11 and 17 Å. By cooling the peptide solution to 80 K in order to reduce the water absorbance the bandwidth was increased to 0.1-3.0 THz for both THz-TDS and FTIR. Spectra were consistent with monotonic absorbance of the peptide and the existence of a solid amorphous low density solvation shell.

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    [CrossRef] [PubMed]
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    [CrossRef]
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    [CrossRef]
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    [CrossRef] [PubMed]
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    [CrossRef] [PubMed]
  8. 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(1-2), 42–48 (2000).
    [CrossRef]
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    [CrossRef] [PubMed]
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    [CrossRef]
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    [CrossRef]
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    [CrossRef]
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    [CrossRef] [PubMed]
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    [CrossRef]
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    [CrossRef]
  28. A. H. Xie, Q. He, L. Miller, B. Sclavi, and M. R. Chance, “Low frequency vibrations of amino acid homopolymers observed by synchrotron far-IR absorption spectroscopy: Excited state effects dominate the temperature dependence of the spectra,” Biopolymers 49(7), 591–603 (1999).
    [CrossRef]
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    [CrossRef]
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    [CrossRef] [PubMed]
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    [CrossRef] [PubMed]
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    [CrossRef] [PubMed]
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    [CrossRef]
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    [CrossRef]
  35. I. Jelesarov, E. Dürr, R. M. Thomas, and H. R. Bosshard, “Salt effects on hydrophobic interaction and charge screening in the folding of a negatively charged peptide to a coiled coil (leucine zipper),” Biochemistry 37(20), 7539–7550 (1998).
    [CrossRef] [PubMed]
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    [CrossRef]
  37. R. J. Falconer, H. A. Zakaria, Y. Y. Fan, A. P. Bradley, and A. P. J. Middelberg, “Far-infrared spectroscopy of protein higher-order structures,” Appl. Spectrosc. 64(11), 1259–1264 (2010).
    [CrossRef] [PubMed]

2010

2009

G. M. Png, R. J. Falconer, B. M. Fischer, H. A. Zakaria, S. P. Mickan, A. P. J. Middelberg, and D. Abbott, “Terahertz spectroscopic differentiation of microstructures in protein gels,” Opt. Express 17(15), 13102–13115 (2009).
[CrossRef] [PubMed]

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 Observation of the Onset of Collective Network Motions,” J. Am. Chem. Soc. 131(10), 3752–3755 (2009).
[CrossRef] [PubMed]

2008

E. Castro-Camus and M. B. Johnston, “Conformational changes of photoactive yellow protein monitored by terahertz spectroscopy,” Chem. Phys. Lett. 455(4-6), 289–292 (2008).
[CrossRef]

Y. F. He, P. I. Ku, J. R. Knab, J. Y. Chen, and A. G. Markelz, “Protein dynamical transition does not require protein structure,” Phys. Rev. Lett. 101(17), 178103 (2008).
[CrossRef] [PubMed]

B. Born, S. J. Kim, S. Ebbinghaus, M. Gruebele, and M. Havenith, “The terahertz dance of water with the proteins: the effect of protein flexibility on the dynamical hydration shell of ubiquitin,” Faraday Discuss. 141, 161–173, discussion 175–207 (2008).
[CrossRef]

T. Arikawa, M. Nagai, and K. Tanaka, “Characterizing hydration state in solution using terahertz time-domain attenuated total reflection spectroscopy,” Chem. Phys. Lett. 457(1-3), 12–17 (2008).
[CrossRef]

A. K. Soper, “Structural transformations in amorphous ice and supercooled water and their relevance to the phase diagram of water,” Mol. Phys. 106(16), 2053–2076 (2008).
[CrossRef]

C. J. Raj, S. Krishnan, S. Dinakaran, R. Uthrakumar, and S. J. Das, “Growth and optical absorption studies on potassium dihydrogen phosphate single crystals,” Cryst. Res. Technol. 43(3), 245–247 (2008).
[CrossRef]

2007

J. A. Zeitler, P. F. Taday, K. C. Gordon, M. Pepper, and T. Rades, “Solid-state transition mechanism in carbamazepine polymorphs by time-resolved terahertz spectroscopy,” ChemPhysChem 8(13), 1924–1927 (2007).
[CrossRef] [PubMed]

J. A. Zeitler, P. F. Taday, M. Pepper, and T. Rades, “Relaxation and crystallization of amorphous carbamazepine studied by terahertz pulsed spectroscopy,” J. Pharm. Sci. 96(10), 2703–2709 (2007).
[CrossRef] [PubMed]

S. C. Shen, L. Santo, and L. Genzel, “THz spectra for some bio-molecules,” Int. J. Infrared Millim. Waves 28(8), 595–610 (2007).
[CrossRef]

M. Nagai, H. Yada, T. Arikawa, and K. Tanaka, “Terahertz time-domain attenuated total reflection spectroscopy in water and biological solution,” Int. J. Infrared Millim. Waves 27(4), 505–515 (2007).
[CrossRef]

A. G. Markelz, J. R. Knab, J. Y. Chen, and Y. F. He, “Protein dynamical transition in terahertz dielectric response,” Chem. Phys. Lett. 442(4-6), 413–417 (2007).
[CrossRef]

W. N. Wang, Y. B. Li, and W. W. Yue, “Vibrational spectrum of histidine and arginine in THz range,” Acta. Phys. Sin. 56, 781–785 (2007).

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,” Proc. Natl. Acad. Sci. U.S.A. 104(52), 20749–20752 (2007).
[CrossRef] [PubMed]

2006

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(5), 1175–1181 (2006).
[CrossRef] [PubMed]

R. Rungsawang, Y. Ueno, I. Tomita, and K. Ajito, “Angle-dependent terahertz time-domain spectroscopy of amino acid single crystals,” J. Phys. Chem. B 110(42), 21259–21263 (2006).
[CrossRef] [PubMed]

F. Haselhuhn, S. Doyle, and M. Kind, “Synchrotron radiation X-ray diffraction study of the particle formation of pseudo-polymorphic calcium oxalate,” J. Cryst. Growth 289(2), 727–733 (2006).
[CrossRef]

P. M. Chaikin, A. Donev, W. Man, F. H Stillinger, and S. Torquato, “Some observations on the random packing of hard ellipoiods,” Ind. Eng. Chem. Res. 45, 6960–6965 (2006).
[CrossRef]

U. Heugen, G. Schwaab, E. Bründermann, M. Heyden, X. Yu, D. M. Leitner, and M. Havenith, “Solute-induced retardation of water dynamics probed directly by terahertz spectroscopy,” Proc. Natl. Acad. Sci. U.S.A. 103(33), 12301–12306 (2006).
[CrossRef] [PubMed]

S. H. Chen, L. Liu, E. Fratini, P. Baglioni, A. Faraone, and E. Mamontov, “Observation of fragile-to-strong dynamic crossover in protein hydration water,” Proc. Natl. Acad. Sci. U.S.A. 103(24), 9012–9016 (2006).
[CrossRef] [PubMed]

2005

B. Fischer, M. Hoffmann, H. Helm, G. Modjesch, and P. U. Jepsen, “Chemical recognition in terahertz time-domain spectroscopy and imaging,” Semicond. Sci. Technol. 20(7), S246–S253 (2005).
[CrossRef]

2003

M. Walther, B. M. Fischer, and P. U. Jepsen, “Noncovalent intermolecular forces in polycrystalline and amorphous saccharides in the far infrared,” Chem. Phys. 288(2-3), 261–268 (2003).
[CrossRef]

2002

M. Walther, P. Plochocka, B. Fischer, H. Helm, and P. Uhd Jepsen, “Collective vibrational modes in biological molecules investigated by terahertz time-domain spectroscopy,” Biopolymers 67(4-5), 310–313 (2002).
[CrossRef] [PubMed]

2001

E. Lindahl, B. Hess, and D. van der Spoel, “GROMACS 3.0: a package for molecular simulation and trajectory analysis,” J. Mol. Model. 7, 306–317 (2001).

2000

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(1-2), 42–48 (2000).
[CrossRef]

1999

A. H. Xie, Q. He, L. Miller, B. Sclavi, and M. R. Chance, “Low frequency vibrations of amino acid homopolymers observed by synchrotron far-IR absorption spectroscopy: Excited state effects dominate the temperature dependence of the spectra,” Biopolymers 49(7), 591–603 (1999).
[CrossRef]

1998

I. Jelesarov, E. Dürr, R. M. Thomas, and H. R. Bosshard, “Salt effects on hydrophobic interaction and charge screening in the folding of a negatively charged peptide to a coiled coil (leucine zipper),” Biochemistry 37(20), 7539–7550 (1998).
[CrossRef] [PubMed]

1994

A. Chakrabartty, T. Kortemme, and R. L. Baldwin, “Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions,” Protein Sci. 3(5), 843–852 (1994).
[CrossRef] [PubMed]

1990

Y. Seno and N. Go, “Deoxymyoglobin studied by the conformational normal mode analysis. II. The conformational change upon oxygenation,” J. Mol. Biol. 216(1), 111–126 (1990).
[CrossRef] [PubMed]

1987

S. Mashimo, S. Kuwabara, S. Yagihara, and K. Higasi, “Dielectric-releaxation time and structure of bound water in biological materials,” J. Phys. Chem. 91(25), 6337–6338 (1987).
[CrossRef]

1985

B. Brooks and M. Karplus, “Normal modes for specific motions of macromolecules: application to the hinge-bending mode of lysozyme,” Proc. Natl. Acad. Sci. U.S.A. 82(15), 4995–4999 (1985).
[CrossRef] [PubMed]

1981

G. W. Chantry, E. A. Nicol, H. A. Willis, and M. E. A. Cudby, “Far infrared studies of the formation of potassium fluoride dihydrate in and its interaction with low molecular weight polytetrafluorethylene,” Int. J. Infrared Millim. Waves 2(1), 97–105 (1981).
[CrossRef]

1976

1974

G. H. Nancollas and G. L. Gardner, “Kinetics of crystal-growth of calcium-oxalate monohydrate,” J. Cryst. Growth 21(2), 267–276 (1974).
[CrossRef]

1969

J. E. Bertie, H. J. Labbe, and E. Whally, “Absorptivity of ice I in range 4000-30 cm-1,” J. Chem. Phys. 50(10), 4501–4520 (1969).
[CrossRef]

Abbott, D.

Ajito, K.

R. Rungsawang, Y. Ueno, I. Tomita, and K. Ajito, “Angle-dependent terahertz time-domain spectroscopy of amino acid single crystals,” J. Phys. Chem. B 110(42), 21259–21263 (2006).
[CrossRef] [PubMed]

Allen, S. J.

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(5), 1175–1181 (2006).
[CrossRef] [PubMed]

Arikawa, T.

T. Arikawa, M. Nagai, and K. Tanaka, “Characterizing hydration state in solution using terahertz time-domain attenuated total reflection spectroscopy,” Chem. Phys. Lett. 457(1-3), 12–17 (2008).
[CrossRef]

M. Nagai, H. Yada, T. Arikawa, and K. Tanaka, “Terahertz time-domain attenuated total reflection spectroscopy in water and biological solution,” Int. J. Infrared Millim. Waves 27(4), 505–515 (2007).
[CrossRef]

Baglioni, P.

S. H. Chen, L. Liu, E. Fratini, P. Baglioni, A. Faraone, and E. Mamontov, “Observation of fragile-to-strong dynamic crossover in protein hydration water,” Proc. Natl. Acad. Sci. U.S.A. 103(24), 9012–9016 (2006).
[CrossRef] [PubMed]

Baldwin, R. L.

A. Chakrabartty, T. Kortemme, and R. L. Baldwin, “Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions,” Protein Sci. 3(5), 843–852 (1994).
[CrossRef] [PubMed]

Bertie, J. E.

J. E. Bertie, H. J. Labbe, and E. Whally, “Absorptivity of ice I in range 4000-30 cm-1,” J. Chem. Phys. 50(10), 4501–4520 (1969).
[CrossRef]

Born, B.

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 Observation of the Onset of Collective Network Motions,” J. Am. Chem. Soc. 131(10), 3752–3755 (2009).
[CrossRef] [PubMed]

B. Born, S. J. Kim, S. Ebbinghaus, M. Gruebele, and M. Havenith, “The terahertz dance of water with the proteins: the effect of protein flexibility on the dynamical hydration shell of ubiquitin,” Faraday Discuss. 141, 161–173, discussion 175–207 (2008).
[CrossRef]

Bosshard, H. R.

I. Jelesarov, E. Dürr, R. M. Thomas, and H. R. Bosshard, “Salt effects on hydrophobic interaction and charge screening in the folding of a negatively charged peptide to a coiled coil (leucine zipper),” Biochemistry 37(20), 7539–7550 (1998).
[CrossRef] [PubMed]

Bradley, A. P.

Brooks, B.

B. Brooks and M. Karplus, “Normal modes for specific motions of macromolecules: application to the hinge-bending mode of lysozyme,” Proc. Natl. Acad. Sci. U.S.A. 82(15), 4995–4999 (1985).
[CrossRef] [PubMed]

Bründermann, E.

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 Observation of the Onset of Collective Network Motions,” J. Am. Chem. Soc. 131(10), 3752–3755 (2009).
[CrossRef] [PubMed]

U. Heugen, G. Schwaab, E. Bründermann, M. Heyden, X. Yu, D. M. Leitner, and M. Havenith, “Solute-induced retardation of water dynamics probed directly by terahertz spectroscopy,” Proc. Natl. Acad. Sci. U.S.A. 103(33), 12301–12306 (2006).
[CrossRef] [PubMed]

Castro-Camus, E.

E. Castro-Camus and M. B. Johnston, “Conformational changes of photoactive yellow protein monitored by terahertz spectroscopy,” Chem. Phys. Lett. 455(4-6), 289–292 (2008).
[CrossRef]

Chaikin, P. M.

P. M. Chaikin, A. Donev, W. Man, F. H Stillinger, and S. Torquato, “Some observations on the random packing of hard ellipoiods,” Ind. Eng. Chem. Res. 45, 6960–6965 (2006).
[CrossRef]

Chakrabartty, A.

A. Chakrabartty, T. Kortemme, and R. L. Baldwin, “Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions,” Protein Sci. 3(5), 843–852 (1994).
[CrossRef] [PubMed]

Chance, M. R.

A. H. Xie, Q. He, L. Miller, B. Sclavi, and M. R. Chance, “Low frequency vibrations of amino acid homopolymers observed by synchrotron far-IR absorption spectroscopy: Excited state effects dominate the temperature dependence of the spectra,” Biopolymers 49(7), 591–603 (1999).
[CrossRef]

Chantry, G. W.

G. W. Chantry, E. A. Nicol, H. A. Willis, and M. E. A. Cudby, “Far infrared studies of the formation of potassium fluoride dihydrate in and its interaction with low molecular weight polytetrafluorethylene,” Int. J. Infrared Millim. Waves 2(1), 97–105 (1981).
[CrossRef]

Chen, J. Y.

Y. F. He, P. I. Ku, J. R. Knab, J. Y. Chen, and A. G. Markelz, “Protein dynamical transition does not require protein structure,” Phys. Rev. Lett. 101(17), 178103 (2008).
[CrossRef] [PubMed]

A. G. Markelz, J. R. Knab, J. Y. Chen, and Y. F. He, “Protein dynamical transition in terahertz dielectric response,” Chem. Phys. Lett. 442(4-6), 413–417 (2007).
[CrossRef]

Chen, S. H.

S. H. Chen, L. Liu, E. Fratini, P. Baglioni, A. Faraone, and E. Mamontov, “Observation of fragile-to-strong dynamic crossover in protein hydration water,” Proc. Natl. Acad. Sci. U.S.A. 103(24), 9012–9016 (2006).
[CrossRef] [PubMed]

Cudby, M. E. A.

G. W. Chantry, E. A. Nicol, H. A. Willis, and M. E. A. Cudby, “Far infrared studies of the formation of potassium fluoride dihydrate in and its interaction with low molecular weight polytetrafluorethylene,” Int. J. Infrared Millim. Waves 2(1), 97–105 (1981).
[CrossRef]

Das, S. J.

C. J. Raj, S. Krishnan, S. Dinakaran, R. Uthrakumar, and S. J. Das, “Growth and optical absorption studies on potassium dihydrogen phosphate single crystals,” Cryst. Res. Technol. 43(3), 245–247 (2008).
[CrossRef]

Dinakaran, S.

C. J. Raj, S. Krishnan, S. Dinakaran, R. Uthrakumar, and S. J. Das, “Growth and optical absorption studies on potassium dihydrogen phosphate single crystals,” Cryst. Res. Technol. 43(3), 245–247 (2008).
[CrossRef]

Donev, A.

P. M. Chaikin, A. Donev, W. Man, F. H Stillinger, and S. Torquato, “Some observations on the random packing of hard ellipoiods,” Ind. Eng. Chem. Res. 45, 6960–6965 (2006).
[CrossRef]

Doyle, S.

F. Haselhuhn, S. Doyle, and M. Kind, “Synchrotron radiation X-ray diffraction study of the particle formation of pseudo-polymorphic calcium oxalate,” J. Cryst. Growth 289(2), 727–733 (2006).
[CrossRef]

Dürr, E.

I. Jelesarov, E. Dürr, R. M. Thomas, and H. R. Bosshard, “Salt effects on hydrophobic interaction and charge screening in the folding of a negatively charged peptide to a coiled coil (leucine zipper),” Biochemistry 37(20), 7539–7550 (1998).
[CrossRef] [PubMed]

Ebbinghaus, S.

B. Born, S. J. Kim, S. Ebbinghaus, M. Gruebele, and M. Havenith, “The terahertz dance of water with the proteins: the effect of protein flexibility on the dynamical hydration shell of ubiquitin,” Faraday Discuss. 141, 161–173, discussion 175–207 (2008).
[CrossRef]

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,” Proc. Natl. Acad. Sci. U.S.A. 104(52), 20749–20752 (2007).
[CrossRef] [PubMed]

Falconer, R. J.

Fan, Y. Y.

Faraone, A.

S. H. Chen, L. Liu, E. Fratini, P. Baglioni, A. Faraone, and E. Mamontov, “Observation of fragile-to-strong dynamic crossover in protein hydration water,” Proc. Natl. Acad. Sci. U.S.A. 103(24), 9012–9016 (2006).
[CrossRef] [PubMed]

Fischer, B.

B. Fischer, M. Hoffmann, H. Helm, G. Modjesch, and P. U. Jepsen, “Chemical recognition in terahertz time-domain spectroscopy and imaging,” Semicond. Sci. Technol. 20(7), S246–S253 (2005).
[CrossRef]

M. Walther, P. Plochocka, B. Fischer, H. Helm, and P. Uhd Jepsen, “Collective vibrational modes in biological molecules investigated by terahertz time-domain spectroscopy,” Biopolymers 67(4-5), 310–313 (2002).
[CrossRef] [PubMed]

Fischer, B. M.

G. M. Png, R. J. Falconer, B. M. Fischer, H. A. Zakaria, S. P. Mickan, A. P. J. Middelberg, and D. Abbott, “Terahertz spectroscopic differentiation of microstructures in protein gels,” Opt. Express 17(15), 13102–13115 (2009).
[CrossRef] [PubMed]

M. Walther, B. M. Fischer, and P. U. Jepsen, “Noncovalent intermolecular forces in polycrystalline and amorphous saccharides in the far infrared,” Chem. Phys. 288(2-3), 261–268 (2003).
[CrossRef]

Fratini, E.

S. H. Chen, L. Liu, E. Fratini, P. Baglioni, A. Faraone, and E. Mamontov, “Observation of fragile-to-strong dynamic crossover in protein hydration water,” Proc. Natl. Acad. Sci. U.S.A. 103(24), 9012–9016 (2006).
[CrossRef] [PubMed]

Gardner, G. L.

G. H. Nancollas and G. L. Gardner, “Kinetics of crystal-growth of calcium-oxalate monohydrate,” J. Cryst. Growth 21(2), 267–276 (1974).
[CrossRef]

Genzel, L.

S. C. Shen, L. Santo, and L. Genzel, “THz spectra for some bio-molecules,” Int. J. Infrared Millim. Waves 28(8), 595–610 (2007).
[CrossRef]

Go, N.

Y. Seno and N. Go, “Deoxymyoglobin studied by the conformational normal mode analysis. II. The conformational change upon oxygenation,” J. Mol. Biol. 216(1), 111–126 (1990).
[CrossRef] [PubMed]

Gordon, K. C.

J. A. Zeitler, P. F. Taday, K. C. Gordon, M. Pepper, and T. Rades, “Solid-state transition mechanism in carbamazepine polymorphs by time-resolved terahertz spectroscopy,” ChemPhysChem 8(13), 1924–1927 (2007).
[CrossRef] [PubMed]

Gruebele, M.

B. Born, S. J. Kim, S. Ebbinghaus, M. Gruebele, and M. Havenith, “The terahertz dance of water with the proteins: the effect of protein flexibility on the dynamical hydration shell of ubiquitin,” Faraday Discuss. 141, 161–173, discussion 175–207 (2008).
[CrossRef]

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,” Proc. Natl. Acad. Sci. U.S.A. 104(52), 20749–20752 (2007).
[CrossRef] [PubMed]

Haselhuhn, F.

F. Haselhuhn, S. Doyle, and M. Kind, “Synchrotron radiation X-ray diffraction study of the particle formation of pseudo-polymorphic calcium oxalate,” J. Cryst. Growth 289(2), 727–733 (2006).
[CrossRef]

Havenith, M.

B. Born, S. J. Kim, S. Ebbinghaus, M. Gruebele, and M. Havenith, “The terahertz dance of water with the proteins: the effect of protein flexibility on the dynamical hydration shell of ubiquitin,” Faraday Discuss. 141, 161–173, discussion 175–207 (2008).
[CrossRef]

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,” Proc. Natl. Acad. Sci. U.S.A. 104(52), 20749–20752 (2007).
[CrossRef] [PubMed]

U. Heugen, G. Schwaab, E. Bründermann, M. Heyden, X. Yu, D. M. Leitner, and M. Havenith, “Solute-induced retardation of water dynamics probed directly by terahertz spectroscopy,” Proc. Natl. Acad. Sci. U.S.A. 103(33), 12301–12306 (2006).
[CrossRef] [PubMed]

Havenith,, M.

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 Observation of the Onset of Collective Network Motions,” J. Am. Chem. Soc. 131(10), 3752–3755 (2009).
[CrossRef] [PubMed]

He, Q.

A. H. Xie, Q. He, L. Miller, B. Sclavi, and M. R. Chance, “Low frequency vibrations of amino acid homopolymers observed by synchrotron far-IR absorption spectroscopy: Excited state effects dominate the temperature dependence of the spectra,” Biopolymers 49(7), 591–603 (1999).
[CrossRef]

He, Y. F.

Y. F. He, P. I. Ku, J. R. Knab, J. Y. Chen, and A. G. Markelz, “Protein dynamical transition does not require protein structure,” Phys. Rev. Lett. 101(17), 178103 (2008).
[CrossRef] [PubMed]

A. G. Markelz, J. R. Knab, J. Y. Chen, and Y. F. He, “Protein dynamical transition in terahertz dielectric response,” Chem. Phys. Lett. 442(4-6), 413–417 (2007).
[CrossRef]

Heilweil, E. J.

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(1-2), 42–48 (2000).
[CrossRef]

Helm, H.

B. Fischer, M. Hoffmann, H. Helm, G. Modjesch, and P. U. Jepsen, “Chemical recognition in terahertz time-domain spectroscopy and imaging,” Semicond. Sci. Technol. 20(7), S246–S253 (2005).
[CrossRef]

M. Walther, P. Plochocka, B. Fischer, H. Helm, and P. Uhd Jepsen, “Collective vibrational modes in biological molecules investigated by terahertz time-domain spectroscopy,” Biopolymers 67(4-5), 310–313 (2002).
[CrossRef] [PubMed]

Hess, B.

E. Lindahl, B. Hess, and D. van der Spoel, “GROMACS 3.0: a package for molecular simulation and trajectory analysis,” J. Mol. Model. 7, 306–317 (2001).

Heugen, U.

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,” Proc. Natl. Acad. Sci. U.S.A. 104(52), 20749–20752 (2007).
[CrossRef] [PubMed]

U. Heugen, G. Schwaab, E. Bründermann, M. Heyden, X. Yu, D. M. Leitner, and M. Havenith, “Solute-induced retardation of water dynamics probed directly by terahertz spectroscopy,” Proc. Natl. Acad. Sci. U.S.A. 103(33), 12301–12306 (2006).
[CrossRef] [PubMed]

Heyden, M.

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,” Proc. Natl. Acad. Sci. U.S.A. 104(52), 20749–20752 (2007).
[CrossRef] [PubMed]

U. Heugen, G. Schwaab, E. Bründermann, M. Heyden, X. Yu, D. M. Leitner, and M. Havenith, “Solute-induced retardation of water dynamics probed directly by terahertz spectroscopy,” Proc. Natl. Acad. Sci. U.S.A. 103(33), 12301–12306 (2006).
[CrossRef] [PubMed]

Higasi, K.

S. Mashimo, S. Kuwabara, S. Yagihara, and K. Higasi, “Dielectric-releaxation time and structure of bound water in biological materials,” J. Phys. Chem. 91(25), 6337–6338 (1987).
[CrossRef]

Hirschfeld, T.

Hoffmann, M.

B. Fischer, M. Hoffmann, H. Helm, G. Modjesch, and P. U. Jepsen, “Chemical recognition in terahertz time-domain spectroscopy and imaging,” Semicond. Sci. Technol. 20(7), S246–S253 (2005).
[CrossRef]

Jelesarov, I.

I. Jelesarov, E. Dürr, R. M. Thomas, and H. R. Bosshard, “Salt effects on hydrophobic interaction and charge screening in the folding of a negatively charged peptide to a coiled coil (leucine zipper),” Biochemistry 37(20), 7539–7550 (1998).
[CrossRef] [PubMed]

Jepsen, P. U.

B. Fischer, M. Hoffmann, H. Helm, G. Modjesch, and P. U. Jepsen, “Chemical recognition in terahertz time-domain spectroscopy and imaging,” Semicond. Sci. Technol. 20(7), S246–S253 (2005).
[CrossRef]

M. Walther, B. M. Fischer, and P. U. Jepsen, “Noncovalent intermolecular forces in polycrystalline and amorphous saccharides in the far infrared,” Chem. Phys. 288(2-3), 261–268 (2003).
[CrossRef]

Johnston, M. B.

E. Castro-Camus and M. B. Johnston, “Conformational changes of photoactive yellow protein monitored by terahertz spectroscopy,” Chem. Phys. Lett. 455(4-6), 289–292 (2008).
[CrossRef]

Karplus, M.

B. Brooks and M. Karplus, “Normal modes for specific motions of macromolecules: application to the hinge-bending mode of lysozyme,” Proc. Natl. Acad. Sci. U.S.A. 82(15), 4995–4999 (1985).
[CrossRef] [PubMed]

Kim, S. J.

B. Born, S. J. Kim, S. Ebbinghaus, M. Gruebele, and M. Havenith, “The terahertz dance of water with the proteins: the effect of protein flexibility on the dynamical hydration shell of ubiquitin,” Faraday Discuss. 141, 161–173, discussion 175–207 (2008).
[CrossRef]

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,” Proc. Natl. Acad. Sci. U.S.A. 104(52), 20749–20752 (2007).
[CrossRef] [PubMed]

Kind, M.

F. Haselhuhn, S. Doyle, and M. Kind, “Synchrotron radiation X-ray diffraction study of the particle formation of pseudo-polymorphic calcium oxalate,” J. Cryst. Growth 289(2), 727–733 (2006).
[CrossRef]

Knab, J. R.

Y. F. He, P. I. Ku, J. R. Knab, J. Y. Chen, and A. G. Markelz, “Protein dynamical transition does not require protein structure,” Phys. Rev. Lett. 101(17), 178103 (2008).
[CrossRef] [PubMed]

A. G. Markelz, J. R. Knab, J. Y. Chen, and Y. F. He, “Protein dynamical transition in terahertz dielectric response,” Chem. Phys. Lett. 442(4-6), 413–417 (2007).
[CrossRef]

Kortemme, T.

A. Chakrabartty, T. Kortemme, and R. L. Baldwin, “Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions,” Protein Sci. 3(5), 843–852 (1994).
[CrossRef] [PubMed]

Krishnan, S.

C. J. Raj, S. Krishnan, S. Dinakaran, R. Uthrakumar, and S. J. Das, “Growth and optical absorption studies on potassium dihydrogen phosphate single crystals,” Cryst. Res. Technol. 43(3), 245–247 (2008).
[CrossRef]

Ku, P. I.

Y. F. He, P. I. Ku, J. R. Knab, J. Y. Chen, and A. G. Markelz, “Protein dynamical transition does not require protein structure,” Phys. Rev. Lett. 101(17), 178103 (2008).
[CrossRef] [PubMed]

Kuwabara, S.

S. Mashimo, S. Kuwabara, S. Yagihara, and K. Higasi, “Dielectric-releaxation time and structure of bound water in biological materials,” J. Phys. Chem. 91(25), 6337–6338 (1987).
[CrossRef]

Labbe, H. J.

J. E. Bertie, H. J. Labbe, and E. Whally, “Absorptivity of ice I in range 4000-30 cm-1,” J. Chem. Phys. 50(10), 4501–4520 (1969).
[CrossRef]

Leitner, D. M.

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,” Proc. Natl. Acad. Sci. U.S.A. 104(52), 20749–20752 (2007).
[CrossRef] [PubMed]

U. Heugen, G. Schwaab, E. Bründermann, M. Heyden, X. Yu, D. M. Leitner, and M. Havenith, “Solute-induced retardation of water dynamics probed directly by terahertz spectroscopy,” Proc. Natl. Acad. Sci. U.S.A. 103(33), 12301–12306 (2006).
[CrossRef] [PubMed]

Li, Y. B.

W. N. Wang, Y. B. Li, and W. W. Yue, “Vibrational spectrum of histidine and arginine in THz range,” Acta. Phys. Sin. 56, 781–785 (2007).

Lindahl, E.

E. Lindahl, B. Hess, and D. van der Spoel, “GROMACS 3.0: a package for molecular simulation and trajectory analysis,” J. Mol. Model. 7, 306–317 (2001).

Liu, L.

S. H. Chen, L. Liu, E. Fratini, P. Baglioni, A. Faraone, and E. Mamontov, “Observation of fragile-to-strong dynamic crossover in protein hydration water,” Proc. Natl. Acad. Sci. U.S.A. 103(24), 9012–9016 (2006).
[CrossRef] [PubMed]

Mamontov, E.

S. H. Chen, L. Liu, E. Fratini, P. Baglioni, A. Faraone, and E. Mamontov, “Observation of fragile-to-strong dynamic crossover in protein hydration water,” Proc. Natl. Acad. Sci. U.S.A. 103(24), 9012–9016 (2006).
[CrossRef] [PubMed]

Man, W.

P. M. Chaikin, A. Donev, W. Man, F. H Stillinger, and S. Torquato, “Some observations on the random packing of hard ellipoiods,” Ind. Eng. Chem. Res. 45, 6960–6965 (2006).
[CrossRef]

Mantz, A. W.

Markelz, A. G.

Y. F. He, P. I. Ku, J. R. Knab, J. Y. Chen, and A. G. Markelz, “Protein dynamical transition does not require protein structure,” Phys. Rev. Lett. 101(17), 178103 (2008).
[CrossRef] [PubMed]

A. G. Markelz, J. R. Knab, J. Y. Chen, and Y. F. He, “Protein dynamical transition in terahertz dielectric response,” Chem. Phys. Lett. 442(4-6), 413–417 (2007).
[CrossRef]

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(1-2), 42–48 (2000).
[CrossRef]

Mashimo, S.

S. Mashimo, S. Kuwabara, S. Yagihara, and K. Higasi, “Dielectric-releaxation time and structure of bound water in biological materials,” J. Phys. Chem. 91(25), 6337–6338 (1987).
[CrossRef]

Mickan, S. P.

Middelberg, A. P. J.

Miller, L.

A. H. Xie, Q. He, L. Miller, B. Sclavi, and M. R. Chance, “Low frequency vibrations of amino acid homopolymers observed by synchrotron far-IR absorption spectroscopy: Excited state effects dominate the temperature dependence of the spectra,” Biopolymers 49(7), 591–603 (1999).
[CrossRef]

Modjesch, G.

B. Fischer, M. Hoffmann, H. Helm, G. Modjesch, and P. U. Jepsen, “Chemical recognition in terahertz time-domain spectroscopy and imaging,” Semicond. Sci. Technol. 20(7), S246–S253 (2005).
[CrossRef]

Nagai, M.

T. Arikawa, M. Nagai, and K. Tanaka, “Characterizing hydration state in solution using terahertz time-domain attenuated total reflection spectroscopy,” Chem. Phys. Lett. 457(1-3), 12–17 (2008).
[CrossRef]

M. Nagai, H. Yada, T. Arikawa, and K. Tanaka, “Terahertz time-domain attenuated total reflection spectroscopy in water and biological solution,” Int. J. Infrared Millim. Waves 27(4), 505–515 (2007).
[CrossRef]

Nancollas, G. H.

G. H. Nancollas and G. L. Gardner, “Kinetics of crystal-growth of calcium-oxalate monohydrate,” J. Cryst. Growth 21(2), 267–276 (1974).
[CrossRef]

Nicol, E. A.

G. W. Chantry, E. A. Nicol, H. A. Willis, and M. E. A. Cudby, “Far infrared studies of the formation of potassium fluoride dihydrate in and its interaction with low molecular weight polytetrafluorethylene,” Int. J. Infrared Millim. Waves 2(1), 97–105 (1981).
[CrossRef]

Pepper, M.

J. A. Zeitler, P. F. Taday, M. Pepper, and T. Rades, “Relaxation and crystallization of amorphous carbamazepine studied by terahertz pulsed spectroscopy,” J. Pharm. Sci. 96(10), 2703–2709 (2007).
[CrossRef] [PubMed]

J. A. Zeitler, P. F. Taday, K. C. Gordon, M. Pepper, and T. Rades, “Solid-state transition mechanism in carbamazepine polymorphs by time-resolved terahertz spectroscopy,” ChemPhysChem 8(13), 1924–1927 (2007).
[CrossRef] [PubMed]

Plaxco, K. W.

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(5), 1175–1181 (2006).
[CrossRef] [PubMed]

Plochocka, P.

M. Walther, P. Plochocka, B. Fischer, H. Helm, and P. Uhd Jepsen, “Collective vibrational modes in biological molecules investigated by terahertz time-domain spectroscopy,” Biopolymers 67(4-5), 310–313 (2002).
[CrossRef] [PubMed]

Png, G. M.

Rades, T.

J. A. Zeitler, P. F. Taday, M. Pepper, and T. Rades, “Relaxation and crystallization of amorphous carbamazepine studied by terahertz pulsed spectroscopy,” J. Pharm. Sci. 96(10), 2703–2709 (2007).
[CrossRef] [PubMed]

J. A. Zeitler, P. F. Taday, K. C. Gordon, M. Pepper, and T. Rades, “Solid-state transition mechanism in carbamazepine polymorphs by time-resolved terahertz spectroscopy,” ChemPhysChem 8(13), 1924–1927 (2007).
[CrossRef] [PubMed]

Raj, C. J.

C. J. Raj, S. Krishnan, S. Dinakaran, R. Uthrakumar, and S. J. Das, “Growth and optical absorption studies on potassium dihydrogen phosphate single crystals,” Cryst. Res. Technol. 43(3), 245–247 (2008).
[CrossRef]

Roitberg, A.

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(1-2), 42–48 (2000).
[CrossRef]

Rungsawang, R.

R. Rungsawang, Y. Ueno, I. Tomita, and K. Ajito, “Angle-dependent terahertz time-domain spectroscopy of amino acid single crystals,” J. Phys. Chem. B 110(42), 21259–21263 (2006).
[CrossRef] [PubMed]

Santo, L.

S. C. Shen, L. Santo, and L. Genzel, “THz spectra for some bio-molecules,” Int. J. Infrared Millim. Waves 28(8), 595–610 (2007).
[CrossRef]

Schwaab, G.

U. Heugen, G. Schwaab, E. Bründermann, M. Heyden, X. Yu, D. M. Leitner, and M. Havenith, “Solute-induced retardation of water dynamics probed directly by terahertz spectroscopy,” Proc. Natl. Acad. Sci. U.S.A. 103(33), 12301–12306 (2006).
[CrossRef] [PubMed]

Sclavi, B.

A. H. Xie, Q. He, L. Miller, B. Sclavi, and M. R. Chance, “Low frequency vibrations of amino acid homopolymers observed by synchrotron far-IR absorption spectroscopy: Excited state effects dominate the temperature dependence of the spectra,” Biopolymers 49(7), 591–603 (1999).
[CrossRef]

Seno, Y.

Y. Seno and N. Go, “Deoxymyoglobin studied by the conformational normal mode analysis. II. The conformational change upon oxygenation,” J. Mol. Biol. 216(1), 111–126 (1990).
[CrossRef] [PubMed]

Shen, S. C.

S. C. Shen, L. Santo, and L. Genzel, “THz spectra for some bio-molecules,” Int. J. Infrared Millim. Waves 28(8), 595–610 (2007).
[CrossRef]

Soper, A. K.

A. K. Soper, “Structural transformations in amorphous ice and supercooled water and their relevance to the phase diagram of water,” Mol. Phys. 106(16), 2053–2076 (2008).
[CrossRef]

Stillinger, F. H

P. M. Chaikin, A. Donev, W. Man, F. H Stillinger, and S. Torquato, “Some observations on the random packing of hard ellipoiods,” Ind. Eng. Chem. Res. 45, 6960–6965 (2006).
[CrossRef]

Taday, P. F.

J. A. Zeitler, P. F. Taday, M. Pepper, and T. Rades, “Relaxation and crystallization of amorphous carbamazepine studied by terahertz pulsed spectroscopy,” J. Pharm. Sci. 96(10), 2703–2709 (2007).
[CrossRef] [PubMed]

J. A. Zeitler, P. F. Taday, K. C. Gordon, M. Pepper, and T. Rades, “Solid-state transition mechanism in carbamazepine polymorphs by time-resolved terahertz spectroscopy,” ChemPhysChem 8(13), 1924–1927 (2007).
[CrossRef] [PubMed]

Tanaka, K.

T. Arikawa, M. Nagai, and K. Tanaka, “Characterizing hydration state in solution using terahertz time-domain attenuated total reflection spectroscopy,” Chem. Phys. Lett. 457(1-3), 12–17 (2008).
[CrossRef]

M. Nagai, H. Yada, T. Arikawa, and K. Tanaka, “Terahertz time-domain attenuated total reflection spectroscopy in water and biological solution,” Int. J. Infrared Millim. Waves 27(4), 505–515 (2007).
[CrossRef]

Thomas, R. M.

I. Jelesarov, E. Dürr, R. M. Thomas, and H. R. Bosshard, “Salt effects on hydrophobic interaction and charge screening in the folding of a negatively charged peptide to a coiled coil (leucine zipper),” Biochemistry 37(20), 7539–7550 (1998).
[CrossRef] [PubMed]

Tomita, I.

R. Rungsawang, Y. Ueno, I. Tomita, and K. Ajito, “Angle-dependent terahertz time-domain spectroscopy of amino acid single crystals,” J. Phys. Chem. B 110(42), 21259–21263 (2006).
[CrossRef] [PubMed]

Torquato, S.

P. M. Chaikin, A. Donev, W. Man, F. H Stillinger, and S. Torquato, “Some observations on the random packing of hard ellipoiods,” Ind. Eng. Chem. Res. 45, 6960–6965 (2006).
[CrossRef]

Ueno, Y.

R. Rungsawang, Y. Ueno, I. Tomita, and K. Ajito, “Angle-dependent terahertz time-domain spectroscopy of amino acid single crystals,” J. Phys. Chem. B 110(42), 21259–21263 (2006).
[CrossRef] [PubMed]

Uhd Jepsen, P.

M. Walther, P. Plochocka, B. Fischer, H. Helm, and P. Uhd Jepsen, “Collective vibrational modes in biological molecules investigated by terahertz time-domain spectroscopy,” Biopolymers 67(4-5), 310–313 (2002).
[CrossRef] [PubMed]

Uthrakumar, R.

C. J. Raj, S. Krishnan, S. Dinakaran, R. Uthrakumar, and S. J. Das, “Growth and optical absorption studies on potassium dihydrogen phosphate single crystals,” Cryst. Res. Technol. 43(3), 245–247 (2008).
[CrossRef]

van der Spoel, D.

E. Lindahl, B. Hess, and D. van der Spoel, “GROMACS 3.0: a package for molecular simulation and trajectory analysis,” J. Mol. Model. 7, 306–317 (2001).

Walther, M.

M. Walther, B. M. Fischer, and P. U. Jepsen, “Noncovalent intermolecular forces in polycrystalline and amorphous saccharides in the far infrared,” Chem. Phys. 288(2-3), 261–268 (2003).
[CrossRef]

M. Walther, P. Plochocka, B. Fischer, H. Helm, and P. Uhd Jepsen, “Collective vibrational modes in biological molecules investigated by terahertz time-domain spectroscopy,” Biopolymers 67(4-5), 310–313 (2002).
[CrossRef] [PubMed]

Wang, W. N.

W. N. Wang, Y. B. Li, and W. W. Yue, “Vibrational spectrum of histidine and arginine in THz range,” Acta. Phys. Sin. 56, 781–785 (2007).

Weingärtner, H.

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 Observation of the Onset of Collective Network Motions,” J. Am. Chem. Soc. 131(10), 3752–3755 (2009).
[CrossRef] [PubMed]

Whally, E.

J. E. Bertie, H. J. Labbe, and E. Whally, “Absorptivity of ice I in range 4000-30 cm-1,” J. Chem. Phys. 50(10), 4501–4520 (1969).
[CrossRef]

Willis, H. A.

G. W. Chantry, E. A. Nicol, H. A. Willis, and M. E. A. Cudby, “Far infrared studies of the formation of potassium fluoride dihydrate in and its interaction with low molecular weight polytetrafluorethylene,” Int. J. Infrared Millim. Waves 2(1), 97–105 (1981).
[CrossRef]

Xie, A. H.

A. H. Xie, Q. He, L. Miller, B. Sclavi, and M. R. Chance, “Low frequency vibrations of amino acid homopolymers observed by synchrotron far-IR absorption spectroscopy: Excited state effects dominate the temperature dependence of the spectra,” Biopolymers 49(7), 591–603 (1999).
[CrossRef]

Xu, J.

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(5), 1175–1181 (2006).
[CrossRef] [PubMed]

Yada, H.

M. Nagai, H. Yada, T. Arikawa, and K. Tanaka, “Terahertz time-domain attenuated total reflection spectroscopy in water and biological solution,” Int. J. Infrared Millim. Waves 27(4), 505–515 (2007).
[CrossRef]

Yagihara, S.

S. Mashimo, S. Kuwabara, S. Yagihara, and K. Higasi, “Dielectric-releaxation time and structure of bound water in biological materials,” J. Phys. Chem. 91(25), 6337–6338 (1987).
[CrossRef]

Yu, X.

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,” Proc. Natl. Acad. Sci. U.S.A. 104(52), 20749–20752 (2007).
[CrossRef] [PubMed]

U. Heugen, G. Schwaab, E. Bründermann, M. Heyden, X. Yu, D. M. Leitner, and M. Havenith, “Solute-induced retardation of water dynamics probed directly by terahertz spectroscopy,” Proc. Natl. Acad. Sci. U.S.A. 103(33), 12301–12306 (2006).
[CrossRef] [PubMed]

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W. N. Wang, Y. B. Li, and W. W. Yue, “Vibrational spectrum of histidine and arginine in THz range,” Acta. Phys. Sin. 56, 781–785 (2007).

Zakaria, H. A.

Zeitler, J. A.

J. A. Zeitler, P. F. Taday, M. Pepper, and T. Rades, “Relaxation and crystallization of amorphous carbamazepine studied by terahertz pulsed spectroscopy,” J. Pharm. Sci. 96(10), 2703–2709 (2007).
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Acta. Phys. Sin.

W. N. Wang, Y. B. Li, and W. W. Yue, “Vibrational spectrum of histidine and arginine in THz range,” Acta. Phys. Sin. 56, 781–785 (2007).

Appl. Spectrosc.

Biochemistry

I. Jelesarov, E. Dürr, R. M. Thomas, and H. R. Bosshard, “Salt effects on hydrophobic interaction and charge screening in the folding of a negatively charged peptide to a coiled coil (leucine zipper),” Biochemistry 37(20), 7539–7550 (1998).
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Biopolymers

A. H. Xie, Q. He, L. Miller, B. Sclavi, and M. R. Chance, “Low frequency vibrations of amino acid homopolymers observed by synchrotron far-IR absorption spectroscopy: Excited state effects dominate the temperature dependence of the spectra,” Biopolymers 49(7), 591–603 (1999).
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Chem. Phys.

M. Walther, B. M. Fischer, and P. U. Jepsen, “Noncovalent intermolecular forces in polycrystalline and amorphous saccharides in the far infrared,” Chem. Phys. 288(2-3), 261–268 (2003).
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Chem. Phys. Lett.

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(1-2), 42–48 (2000).
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A. G. Markelz, J. R. Knab, J. Y. Chen, and Y. F. He, “Protein dynamical transition in terahertz dielectric response,” Chem. Phys. Lett. 442(4-6), 413–417 (2007).
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T. Arikawa, M. Nagai, and K. Tanaka, “Characterizing hydration state in solution using terahertz time-domain attenuated total reflection spectroscopy,” Chem. Phys. Lett. 457(1-3), 12–17 (2008).
[CrossRef]

ChemPhysChem

J. A. Zeitler, P. F. Taday, K. C. Gordon, M. Pepper, and T. Rades, “Solid-state transition mechanism in carbamazepine polymorphs by time-resolved terahertz spectroscopy,” ChemPhysChem 8(13), 1924–1927 (2007).
[CrossRef] [PubMed]

Cryst. Res. Technol.

C. J. Raj, S. Krishnan, S. Dinakaran, R. Uthrakumar, and S. J. Das, “Growth and optical absorption studies on potassium dihydrogen phosphate single crystals,” Cryst. Res. Technol. 43(3), 245–247 (2008).
[CrossRef]

Faraday Discuss.

B. Born, S. J. Kim, S. Ebbinghaus, M. Gruebele, and M. Havenith, “The terahertz dance of water with the proteins: the effect of protein flexibility on the dynamical hydration shell of ubiquitin,” Faraday Discuss. 141, 161–173, discussion 175–207 (2008).
[CrossRef]

Ind. Eng. Chem. Res.

P. M. Chaikin, A. Donev, W. Man, F. H Stillinger, and S. Torquato, “Some observations on the random packing of hard ellipoiods,” Ind. Eng. Chem. Res. 45, 6960–6965 (2006).
[CrossRef]

Int. J. Infrared Millim. Waves

G. W. Chantry, E. A. Nicol, H. A. Willis, and M. E. A. Cudby, “Far infrared studies of the formation of potassium fluoride dihydrate in and its interaction with low molecular weight polytetrafluorethylene,” Int. J. Infrared Millim. Waves 2(1), 97–105 (1981).
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M. Nagai, H. Yada, T. Arikawa, and K. Tanaka, “Terahertz time-domain attenuated total reflection spectroscopy in water and biological solution,” Int. J. Infrared Millim. Waves 27(4), 505–515 (2007).
[CrossRef]

J. Am. Chem. Soc.

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 Observation of the Onset of Collective Network Motions,” J. Am. Chem. Soc. 131(10), 3752–3755 (2009).
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J. Cryst. Growth

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J. Pharm. Sci.

J. A. Zeitler, P. F. Taday, M. Pepper, and T. Rades, “Relaxation and crystallization of amorphous carbamazepine studied by terahertz pulsed spectroscopy,” J. Pharm. Sci. 96(10), 2703–2709 (2007).
[CrossRef] [PubMed]

J. Phys. Chem.

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[CrossRef]

J. Phys. Chem. B

R. Rungsawang, Y. Ueno, I. Tomita, and K. Ajito, “Angle-dependent terahertz time-domain spectroscopy of amino acid single crystals,” J. Phys. Chem. B 110(42), 21259–21263 (2006).
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Mol. Phys.

A. K. Soper, “Structural transformations in amorphous ice and supercooled water and their relevance to the phase diagram of water,” Mol. Phys. 106(16), 2053–2076 (2008).
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Opt. Express

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Y. F. He, P. I. Ku, J. R. Knab, J. Y. Chen, and A. G. Markelz, “Protein dynamical transition does not require protein structure,” Phys. Rev. Lett. 101(17), 178103 (2008).
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Proc. Natl. Acad. Sci. U.S.A.

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,” Proc. Natl. Acad. Sci. U.S.A. 104(52), 20749–20752 (2007).
[CrossRef] [PubMed]

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[CrossRef] [PubMed]

U. Heugen, G. Schwaab, E. Bründermann, M. Heyden, X. Yu, D. M. Leitner, and M. Havenith, “Solute-induced retardation of water dynamics probed directly by terahertz spectroscopy,” Proc. Natl. Acad. Sci. U.S.A. 103(33), 12301–12306 (2006).
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[CrossRef]

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Figures (8)

Fig. 1
Fig. 1

The terahertz time-domain spectroscopy (THz-TDS) arrangement.

Fig. 2
Fig. 2

THz-TDS measurements of peptide samples at room temperature. A) 25 mM AK17 B) 25 mM AK10G and C) 25 mM AK9P in 0.1 M KF solution, windows of the measuring cell are used as the reference. The respective buffer absorption is also shown in black and the peptide solution absorption shown in grey. The black dot line estimated absorption of buffer considering the volume exclusion effect exerted by the peptide. The error bars represent instrument error.

Fig. 3
Fig. 3

Room temperature THz-TDS measurements of peptide solution absorbance relative to KF buffer. Data points from 0.2 to 1.5 THz were used. The experimental result are shown as solid lines and the modelling result are shown as dot lines. AK17 (green), AK10G (blue) and AK9P (red). The error bars represent instrument error.

Fig. 4
Fig. 4

Peptide (AK17, AK10G and AK9P) conformation at 1, 5, 5.5 and 6 ns of simulation by Gromacs software showing differences in peptide conformation and structural stabilization after 5 ns of simulation.

Fig. 5
Fig. 5

THz-TDs measurements of low temperature liquid. Experiments were performed at 79 K: A) AK17 in KF buffer, B) AK10G in KF buffer, C) AK9P in KF buffer. The 50 mM sample is shown in blue, 25 mM sample is shown in green and 12.5 mM sample is shown in red. The buffer line is shown as a dot ted line. D) Concentration dependence of AK17, AK10G and AK9P, data point at 2 THz was used. The error bars represent instrument error.

Fig. 6
Fig. 6

A comparison of absorption spectra from THz-TDS setup (grey) and FTIR setup (black). A) KF buffer. The arrows indicate the phonon-like resonance found in both measurements. B) 50 mM AK17 in KF buffer. Data were collected at 80 K.

Fig. 7
Fig. 7

The FTIR measurement of AK 17 peptide dissolved in 10 mM phosphate buffer, measured at 79 K. Red: 50 mM AK17, Blue: 25 mM AK17, Green: 12.5 mM AK17, Yellow: 6.25 mM AK17, black dot: buffer.

Fig. 8
Fig. 8

The effect of different concentration of peptide on the salt crystallization. Data points are collected from FTIR measurements at 79 K. Peak height at 87 cm−1 is extracted against the absorption baseline and plotted against the peptide concentrations. Red: AK17, Blue: AK10G, Green: AK9P and Black: AQ17.

Tables (1)

Tables Icon

Table 1 The four peptide’s amino acid sequence, helicity (from literature and measured by circular dichroism spectroscopy), radius of gyration (calculated) and apparent solvation shell thickness (experimental).

Equations (3)

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P e x c l u d e d = N s o l u t e V e x c l u d e d V s o l u t i o n
A e x c l u d e d = A buffer ( 1 P e x c l u d e d )
A r = i = 1 N = 59 ( ( A s a m p l e ) i / ( A buffer ) i ) N

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