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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.

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Portable Document Format (PDF) file https://doi.org/10.1107/S1600576713029506/fs5051sup1.pdf
Supplementary figures illustrating control data and a full temperature sweep at a wider selection of THz frequencies than presented in the main text


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