Probing temperature- and solvent-dependent protein dynamics using terahertz time-domain spectroscopy

被引：2
|
作者：
Tych, Katarzyna M. [1 ]
Wood, Christopher D. [1 ]
Burnett, Andrew D. [1 ]
Pearson, Arwen R. [1 ]
Davies, A. Giles [1 ]
Linfield, Edmund H. [1 ]
Cunningham, John E. [1 ]
机构：
[1] Univ Leeds, Astbury Ctr Struct Mol Biol, Leeds LS2 9JT, W Yorkshire, England
来源：
JOURNAL OF APPLIED CRYSTALLOGRAPHY | 2014年 / 47卷
基金：
英国工程与自然科学研究理事会;
关键词：
NEUTRON-SCATTERING; MOLECULAR-DYNAMICS; ENZYME-ACTIVITY; TRANSITION; HYDRATION; LYSOZYME; WATER; CRYSTALS; RELAXATION; ABSORPTION;
D O I：
10.1107/S1600576713029506
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
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 similar to 150 K, which is in agreement with literature values measured using differential scanning calorimetry.
引用
收藏
页码：146 / 153
页数：8
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