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| VOLUME 90 | ISSUE 1 |
PAGE 85
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| Protein Dynamics in Brillouin Light Scattering: Termal Denaturation of Hen Egg White Lysozyme
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A. V. Svanidze, S. G. Lushnikov, S. Kojima+
A.F. Ioffe Physical Technical Institute, 194021 St. Petersburg, Russia
+Institute of Materials Science, University of Tsukuba, Tsukuba City, 305-8573 Ibaraki, Japan
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PACS: 78.35.+c, 87.14.Ee, 87.15.-v
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Abstract
Thermal denaturation of hen egg white lysozyme has been
investigated by Brillouin light scattering in the temperature range from 297
to 350 K. Anomalies in the temperature dependences of velocity and damping
of hypersound and also in the behavior of the intensity of Brillouin
components for the lysozyme solution at thermal denaturation have been revealed. These
anomalies are attributable to phase transformations of the protein in the
high-temperature region. It has been shown that Brillouin light scattering is
a suitable tool for studying the structural evolution of proteins.
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