Protein dynamical transition in terahertz dielectric response

Markelz, Andrea; Knab, Joseph R.; Chen, Jing Yin; He, Yan

doi:10.1016/j.cplett.2007.05.080

Cited by 90 publications

(72 citation statements)

References 26 publications

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“…16 A well-defined dynamical transition related to biomolecule functioning above specific hydration levels (27% w/w), or temperatures (above 200 K), is detectable in THz spectrum. [16][17][18][19][20] Another study reveals the existence of structural collective modes for cytochrome c protein. 15 Solvated proteins (lysozyme and bovine serum albumin (BSA)), along with alcohols, have been also studied at different concentrations by micro-fluidic systems 4,21 over 50-110 GHz.…”

Section: Introductionmentioning

confidence: 99%

Sub-terahertz spectroscopy reveals that proteins influence the properties of water at greater distances than previously detected

Sushko¹,

Dubrovka²,

Donnan³

2015

The Journal of Chemical Physics

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Erratum: "Sub-terahertz spectroscopy reveals that proteins influence the properties of water at greater distances than previously detected" [J. Chem. Phys. 142, 055101 (2015) 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 protein 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 protein 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 protein. It is also seen that THz radiation can serve as an initial estimate of the protein hydrophobicity. C 2015 Author(s). All article content, except where otherwise noted, is licensed under a Creative Commons Attribution 3.0 Unported License. [http://dx

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Section: Introductionmentioning

confidence: 99%

Sub-terahertz spectroscopy reveals that proteins influence the properties of water at greater distances than previously detected

Sushko¹,

Dubrovka²,

Donnan³

2015

The Journal of Chemical Physics

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“…This concept was applied to study a wide range of molecular interactions of biomolecules during solvation: lactose; 78 threhalose, lactose, and glucose; 79 among others. In addition, very interesting effects regarding the hydration of biomolecules were detected using terahertz spectroscopy, [90][91][92] including the protein dynamic transition 93,94 and lipid-membrane formation. 95,96 More detailed reviews of these topics have been published.…”

Section: Mesoscopic Structure and Dynamicsmentioning

confidence: 99%

Terahertz Time-Domain and Low-Frequency Raman Spectroscopy of Organic Materials

2015

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With the ongoing proliferation of terahertz time-domain instrumentation from semiconductor physics into applied spectroscopy over the past decade, measurements at terahertz frequencies (1 THz [ 10 12 Hz [ 33 cm À1) have attracted a sustained growing interest, in particular the investigation of hydrogen-bonding interactions in organic materials. More recently, the availability of Raman spectrometers that are readily able to measure in the equivalent spectral region very close to the elastic scattering background has also grown significantly. This development has led to renewed efforts in performing spectroscopy at the interface between dielectric relaxation phenomena and vibrational spectroscopy. In this review, we briefly outline the underlying technology, the physical phenomena governing the light-matter interaction at terahertz frequencies, recent examples of spectroscopic studies, and the current state of the art in assigning spectral features to vibrational modes based on computational techniques.

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“…This could be particularly useful when considering the practical difficulties in terms of expense and beam time availability to perform neutron scattering measurements, which makes it an unsuitable technique for routine analysis of a large number of samples. As an example, neutron scattering has proven to be useful in determining the dynamical transition of solvated proteins by examining the means square displacement u 2 [27] and it has been since demonstrated that similar information can be extracted using THz-TDS [28,29].…”

Section: Comparison Of Terahertz Spectroscopy To Scattering Techniquesmentioning

confidence: 99%

Terahertz response of organic amorphous systems: experimental concerns and perspectives

Šibík

Zeitler

2015

Philosophical Magazine

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We summarize practical considerations for performing highly accurate terahertz spectroscopy measurements of amorphous systems. We also outline possible perspectives for a further development of terahertz spectroscopy and its applications. This includes a deeper understanding of terahertz dynamics of amorphous systems and the development of a theory for a comparison of terahertz spectra to the results commonly obtained from well-established scattering experiments.

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Protein dynamical transition in terahertz dielectric response

Cited by 90 publications

References 26 publications

Sub-terahertz spectroscopy reveals that proteins influence the properties of water at greater distances than previously detected

Sub-terahertz spectroscopy reveals that proteins influence the properties of water at greater distances than previously detected

Terahertz Time-Domain and Low-Frequency Raman Spectroscopy of Organic Materials

Terahertz response of organic amorphous systems: experimental concerns and perspectives

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