Using Raman spectroscopy and the lysozyme as model system, we investigate the differences in protein conformation before and after Langmuir- Blodgett nanotemplate-induced crystal nucleation and growth. It was found, that the main difference in lysozyme conformation is associated to the higher amount of S-S bonds in lysozyme of LB crystals, probably in C-end of protein, resulting in the higher stiffness of the lysozyme molecules and LB crystal in a whole. Growth in size of LB crystal over time is also accompanied by the formation of S-S bonds. Atomic structure determined by X-ray diffraction correlates to the above pointing to the main differences between LB classical crystals in terms of water molecules environment previously associated to the increased radiation stability of LB crystals.
Raman spectroscopy of protein crystal nucleation and growth
Eugenia, Pechkova;Fiordoro, Stefano;Claudio, Nicolini
2014-01-01
Abstract
Using Raman spectroscopy and the lysozyme as model system, we investigate the differences in protein conformation before and after Langmuir- Blodgett nanotemplate-induced crystal nucleation and growth. It was found, that the main difference in lysozyme conformation is associated to the higher amount of S-S bonds in lysozyme of LB crystals, probably in C-end of protein, resulting in the higher stiffness of the lysozyme molecules and LB crystal in a whole. Growth in size of LB crystal over time is also accompanied by the formation of S-S bonds. Atomic structure determined by X-ray diffraction correlates to the above pointing to the main differences between LB classical crystals in terms of water molecules environment previously associated to the increased radiation stability of LB crystals.File | Dimensione | Formato | |
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Pechkova Am J Bioch Biotech 2014 .pdf
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