Tych, KM, Wood, CD, Burnett, AD et al. (4 more authors) (2014) Probing temperature- and solvent-dependent protein dynamics using terahertz time-domain spectroscopy. Journal of Applied Crystallography, 47 (1). 146 - 153. ISSN 0021-8898
Abstract
The effect of temperature on the terahertz-frequency-range material properties of lyophilized and single-crystal hen egg-white lysozyme has been measured using terahertz time-domain spectroscopy, with the results presented and discussed in the context of protein and solvent dynamical and glass transitions. Lyophilized hen egg-white lysozyme was measured over a temperature range from 4 to 290 K, and a change in the dynamical behaviour of the sample at around 100 K was observed through a change in the terahertz absorption spectrum. Additionally, the effect of cryoprotectants on the temperature-dependent absorption coefficient is studied, and it is demonstrated that terahertz time-domain spectroscopy is capable of resolving the true glass transition temperature of single-crystal hen egg-white lysozyme at 150 K, which is in agreement with literature values measured using differential scanning calorimetry.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2014, International Union of Crystallography. Reproduced in accordance with the publisher's self-archiving policy. |
Keywords: | Terahertz frequency range; protein crystals; lysozyme; dynamical transitions; glass transitions; cryoprotectants |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Electronic & Electrical Engineering (Leeds) > Pollard Institute (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 13 Mar 2014 16:26 |
Last Modified: | 19 Jan 2018 22:13 |
Published Version: | http://dx.doi.org/10.1107/S1600576713029506 |
Status: | Published |
Publisher: | International Union of Crystallography |
Refereed: | Yes |
Identification Number: | 10.1107/S1600576713029506 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:78147 |