A rechargeable iron-ion battery (Fe-ion battery) has been fabricated in our laboratory using a pure ionic liquid electrolyte. Magnetic ionic liquids of 1-butyl-3-methylimidazolium tetrachloroferrate (BmimFeCl) and 1-methyl-3-octylimidazolium tetrachloroferrate (OmimFeCl) are synthesized and utilized as electrolytes in this work. The chemical structure of the two ionic liquids (ILs) is investigated using Raman analysis.
View Article and Find Full Text PDFNon-monotonic behavior has been observed in the optoelectronic properties of ZnO thin films as doped with Hf (HZO). Here we propose that two competing mechanisms are responsible for such behaviour. Specifically, we propose that provided two crystal orientations dominate film growth, only one of them might be responsible for direct Hf substitution.
View Article and Find Full Text PDFThe availability of proteomics resources hosting protein and peptide standards, as well as the data describing their analytical performances, will continue to enhance our current capabilities to develop targeted proteomics methods for quantitative biology. This study describes the analysis of a resource of 26,840 individually purified recombinant protein fragments corresponding to more than 16,000 human protein-coding genes. The resource was screened to identify proteotypic peptides suitable for targeted proteomics efforts, and we report LC-MS/MS assay coordinates for more than 25,000 proteotypic peptides, corresponding to more than 10,000 unique proteins.
View Article and Find Full Text PDFJ Chromatogr B Analyt Technol Biomed Life Sci
May 2016
For protein analysis of biological samples, two major strategies are used today; mass spectrometry (MS) and antibody-based methods. Each strategy offers advantages and drawbacks. However, combining the two using an immunoenrichment step with MS analysis brings together the benefits of each method resulting in increased sensitivity, faster analysis and possibility of higher degrees of multiplexing.
View Article and Find Full Text PDFFor identification and characterization of proteins in complex samples, immunoenrichment coupled to mass spectrometry is a good alternative due to the sensitivity of the affinity enrichment and the specificity of mass spectrometry analysis. Antibodies are commonly used affinity agents; however, for high-throughput analysis, antibody availability is usually a bottleneck. Here we present a protocol for immunoenrichment coupled to mass spectrometry in a high-throughput setup, where all steps from bead coupling to mass spectrometry sample preparation are performed in parallel in a 96-well format.
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