phosphoramidite and titanium-dioxide

phosphoramidite has been researched along with titanium-dioxide* in 1 studies

Other Studies

1 other study(ies) available for phosphoramidite and titanium-dioxide

ArticleYear
Mapping of phosphorylation sites by LC-MS/MS.
    Methods in molecular biology (Clifton, N.J.), 2010, Volume: 658

    Reversible protein phosphorylation ranks among the most important post-translational modifications that occurs in the cell. It is therefore highly relevant to elucidate the phosphorylation states of a given biological system, albeit challenging. Most notably the often low stoichiometry of phosphorylation is inherently incompatible with standard LC-MS analysis of a complex protein digest mixture, primarily due to the relative low dynamic range of current mass analyzers. Therefore a need for specific enrichment of phosphorylated peptides or proteins exists. Significant progress surrounding the biochemical analysis of reversible protein phosphorylation in the past years has led to the development of several new techniques to isolate or enrich phosphopeptides, particularly in large-scale analyses. This chapter deals with three such examples.

    Topics: Analytic Sample Preparation Methods; Binding Sites; Chromatography, Affinity; Chromatography, Liquid; Databases, Protein; Dendrimers; Microspheres; Organophosphorus Compounds; Peptide Fragments; Phosphoproteins; Phosphorylation; Proteins; Tandem Mass Spectrometry; Titanium

2010