Raman Spectroscopy of Protein Crystal Nucleation and Growth
Pechkova Eugenia, Maksimov, Georgy, Parshina Evgenia, Maksimov Evgenii, Kutusov Nikolai, Brazhe Nadezda, Tarasova Irina, Stefano Fiordoro and Nicolini Claudio
DOI : 10.3844/ajbbsp.2014.202.207
American Journal of Biochemistry and Biotechnology
Volume 10, Issue 3
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.
© 2014 Pechkova Eugenia, Maksimov, Georgy, Parshina Evgenia, Maksimov Evgenii, Kutusov Nikolai, Brazhe Nadezda, Tarasova Irina, Stefano Fiordoro and Nicolini Claudio. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.