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Metodo per la crescita accelerata di cristalli proteici su film sottili proteici omologhi
No full textNew Trends in Protein Nanocrystallography Based On LB Nanotemplate, Cell Free Expression, SNAP APA and Montecarlo: A Review
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From art to science in protein crystallography by means of nanotechnology - one year later
No full textFrom Nanobiotechnology to Organic and Biological Monitoring of Health and Environment for Biosafety
No full textThis overview describes the optimal implementation and utilization of different, newly conceived nanosensors for human biosafety purposes, exploiting a variety of methods (amperometric, conductometric, spectrometric and nanogravimetric), and a wide range of nanocomposites, genes and recombinant enzymes. Namely, while biological nanosensors were designed based on Nucleic Acid Programmable Protein Arrays (NAPPA), with or without SNAPtag, and on Langmuir-Blodgett (LB) thin films of recombinant laccase (Rigidoporus lignosus, formerly known as Rigidoporus microporus), organic nanosensors were based on matrices of calcium oxide (CaO) and on carbon nanotubes-either multi-walled (MWNTs) or single-walled (SWNTs)- embedded in poly(o-methylaniline) (POTO). Special attention was paid both to detecting useful and relevant substances (such as carbon dioxide, phenols and phenolic derivatives and compounds) and designing devices and molecules for human biosafety like vaccines and others, by means of amperometry, conductimetry, mass spectrometry (MS) and other label-free technologies, such as quartz crystal microbalance with dissipation monitoring (QCM_D)
SpADS and SNAP-NAPPA Microarrays towards Biomarkers Identification in Humans: Background Subtraction in Mass Spectrometry with E.coli Cell Free Expression System
No full textWe present a useful approach towards for biomarkers identification in an innovative self-assembling protein microarray based on “Nucleic Acid Programmable Protein Array” (NAPPA) and SNAP tag coupled to E.coli cell free expression system. This approach prove capable to resolve the “background” problem associated to the above label free detection system for the identification of proteins and of protein-protein interaction in humans that could become used in clinical practice
In situ monitoring by Raman spectroscopy of lysozyme conformation during "Nanotemplate" induced crystallization
No full textUsing 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
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