科研之友
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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.
- 出版日期2011-6
