Anomalous behavior of Brillouin light scattering at thermal denaturation of lysozyme |
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Authors: | A V Svanidze V P Romanov S G Lushnikov |
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Institution: | 1. Faculty of Physics, St. Petersburg State University, St. Petersburg, 198504, Russia 2. Ioffe Physical Technical Institute, Russian Academy of Sciences, Politekhnicheskaya ul. 26, St. Petersburg, 194021, Russia
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Abstract: | 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 180° scattering geometry and almost complete their disappearance in the case of the 90° 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. |
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