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VOLUME 90 (2009) | ISSUE 1 | PAGE 85
Protein Dynamics in Brillouin Light Scattering: Termal Denaturation of Hen Egg White Lysozyme
PACS: 78.35.+c, 87.14.Ee, 87.15.-v
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.