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Probing temperature‐ and solvent‐dependent protein dynamics using terahertz time‐domain spectroscopy
Author(s) -
Tych Katarzyna M.,
Wood Christopher D.,
Burnett Andrew D.,
Pearson Arwen R.,
Davies A. Giles,
Linfield Edmund H.,
Cunningham John E.
Publication year - 2014
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s1600576713029506
Subject(s) - terahertz time domain spectroscopy , terahertz radiation , terahertz spectroscopy and technology , differential scanning calorimetry , spectroscopy , context (archaeology) , absorption spectroscopy , analytical chemistry (journal) , materials science , chemistry , atmospheric temperature range , absorption (acoustics) , crystal (programming language) , optics , thermodynamics , physics , optoelectronics , chromatography , paleontology , quantum mechanics , biology , computer science , composite material , programming language
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.