Anomalous behavior of Brillouin light scattering at thermal denaturation of lysozyme

被引:5
|
作者
Svanidze, A. V. [1 ]
Romanov, V. P. [2 ]
Lushnikov, S. G. [2 ]
机构
[1] St Petersburg State Univ, Fac Phys, St Petersburg 198504, Russia
[2] Russian Acad Sci, AF Ioffe Phys Tech Inst, St Petersburg 194021, Russia
基金
俄罗斯基础研究基金会;
关键词
EGG-WHITE LYSOZYME; X-RAY-SCATTERING; BIOLOGICAL MACROMOLECULES; SCANNING CALORIMETRY; GLOBULAR-PROTEINS; SOUND-VELOCITY; TRANSITION; SPECTROSCOPY; DYNAMICS; WATER;
D O I
10.1134/S0021364011070113
中图分类号
O4 [物理学];
学科分类号
0702 ;
摘要
The thermal denaturation of lysozyme heated from 293 to 355 K has been studied using Brillouin light scattering. An anomalous temperature behavior of the velocity and damping of hypersound, which is accompanied by a decrease in the intensity of the Brillouin components in the experiments with the 180A degrees scattering geometry and almost complete their disappearance in the case of the 90A degrees scattering geometry, has been observed at the sol-gel transition in the vicinity of 343 K. Such anomalies in the light scattering spectra are absent for a sodium acetate buffer used to prepare protein solutions. A mechanism describing the behavior of the intensities of the Brillouin components has been proposed.
引用
收藏
页码:409 / 414
页数:6
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