Open AccessIn situ Monitoring By Raman Spectroscopy of Lysozyme Conformation during “Nanotemplate” Induced Crystallization
Author(s) -
Claudio Nicolini,
Luca Belmonte,
Г. В. Максимов,
Nadezda Brazhe,
Eugenia Pechkova
Publication year - 2013
Publication title -
journal of microbial and biochemical technology
Language(s) - English
Resource type - Journals
ISSN - 1948-5948
DOI - 10.4172/1948-5948.1000114
Subject(s) - in situ , crystallization , raman spectroscopy , lysozyme , materials science , chemical engineering , crystallography , chemistry , biophysics , biochemistry , biology , organic chemistry , physics , optics , engineering
Using Raman spectroscopy and lysozyme, this latter as model protein, we investigate the differences in protein conformation before and after LB 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 Raman spectroscopy results confirm the main differences between LB and classical crystals are in terms of water molecules environment previously associated to the increased radiation stability of LB crystals