3 articles for “Langmuir-Blodgett (LB)”

Research ArticleOpen accessEvery word in the titleLANGMUIR-BLODGETT NANOTEMPLATE CRYSTALLIZATION COMBINED TO LASER-MICROFRAGMENTATION UNIQUELY CHARACTERIZE PROTEINS CRYSTALS BY SYNCHROTRON MICRODIFFRACTIONClaudio Nicolini, Luca Belmonte, Christian Riekel et al.Laser-induced microfragmentation of LB nanotemplate-induced protein crystals in glycerol solution results in distinct, coherently diffracting domains. Only crystals produced according to the Langmuir-Blodgett (LB) nanotemplate technique reveal in all four proteins being tested (lysozyme, insulin, thaumatin and ribonuclease) domains highly radiation resistant, while the crystals produced by the standard hanging drop crystallization method do not. Actually the very same laser … …American Journal of Biochemistry and Biotechnology, Vol. 10, Issue 1 · 11 Feb 2014 · 7,989 accessesView PDF Cite

Research ArticleOpen accessEvery word in the titleSynchrotron Powder Diffraction Study of Radiation Damage in Langmuir Blodgett Nanotemplate Crystallised ProteinJonathan P. Wright, Eugenia Pechkova, Claudio NicoliniPolycrystalline samples of lysozyme were prepared with and without a Langmuir-Blodgett (LB) thin film template via both the hanging drop method and batch crystallisation. Powder diffraction methods are used to compare these samples and to measure their resistance to radiation damage at room temperature. The X-ray induced amorphisation of the samples was followed as a function of time and it … …American Journal of Biochemistry and Biotechnology, Vol. 10, Issue 3 · 12 Nov 2014 · 8,177 accessesView PDF Cite

Research ArticleOpen accessIn the abstractRaman Spectroscopy of Protein Crystal Nucleation and GrowthPechkova Eugenia, Maksimov, Georgy et al.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 … …American Journal of Biochemistry and Biotechnology, Vol. 10, Issue 3 · 8 Dec 2014 · 8,279 accessesView PDF Cite