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Study of the Phase Transition in Lysozyme Crystals by Raman Spectroscopy

Study of the Phase Transition in Lysozyme Crystals by Raman Spectroscopy

Anna V Frontzek, Laurent Paccou, Yannick Guinet, Alain Hédoux

Biochim Biophys Acta. 2016 Feb;1860(2):412-23.

PMID: 26518350

Abstract:

Background:
Recently, it has been revealed that tetragonal lysozyme crystals show a phase transition at 307 K upon heating. The underlying mechanisms of the phase transition are still not fully understood. Here we focus on the study of high-frequency vibrational modes arising from the protein and their temperature evolution in the vicinity of Tph as well as on the detailed study of crystalline water dynamics near Tph.
Methods:
Raman experiments have been performed at temperatures 295-323 K including Tph. The low-frequency modes and the modes of fingerprint region, CH- and OH-stretching regions have been analyzed.
Results and conclusions:
In spite of the absence of noticeable rearrangements in protein structure, the high-frequency vibrational modes of lysozyme located in the fingerprint region have been found to exhibit the features of critical dynamics near Tph. Pronounced changes in the dynamics of α-helixes and Tyr residues exposed on the protein surface point to the important role of H-bond rearrangements at the phase transition. Additionally the study of temperature evolution of OH-stretching modes has shown an increase in distortions of tertahedral H-bond network of crystalline water above Tph. These changes in water dynamics could play a crucial role in the mechanisms of the phase transition.
General significance:
The present results shed light on the mechanisms of the phase transition in lysozyme crystals.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AS2121373	TPH in Water			Price

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