Research Article Open Access

Raman Spectroscopy of Protein Crystal Nucleation and Growth

Pechkova Eugenia1, Maksimov2, Georgy2, Parshina Evgenia2, Maksimov Evgenii2, Kutusov Nikolai2, Brazhe Nadezda2, Tarasova Irina2, Stefano Fiordoro1 and Nicolini Claudio1
  • 1 University of Genoa, Italy
  • 2 Moscow State University, Russia

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.

American Journal of Biochemistry and Biotechnology
Volume 10 No. 3, 2014, 202-207

DOI: https://doi.org/10.3844/ajbbsp.2014.202.207

Submitted On: 16 October 2014 Published On: 8 December 2014

How to Cite: Eugenia, P., Maksimov, ., Georgy, ., Evgenia, P., Evgenii, M., Nikolai, K., Nadezda, B., Irina, T., Fiordoro, S. & Claudio, N. (2014). Raman Spectroscopy of Protein Crystal Nucleation and Growth. American Journal of Biochemistry and Biotechnology, 10(3), 202-207. https://doi.org/10.3844/ajbbsp.2014.202.207

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Keywords

  • Raman Spectroscopy
  • Thin LB Films
  • Lysozyme
  • Crystal Growth