Titlebook: Mass Spectrometry of Proteins; Methods and Protocol Caroline A.‘Evans,Phillip C. Wright,Josselin Noire Book 2019 Springer Science+Business

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1064-3745 ation advice from the expertsNew insights into modern medicine and systems biology are enabled by innovative protocols and advanced technologies in mass spectrometry-based proteomics. This volume details new pipelines, workflows, and ways to process data that allow for new frontiers in proteomics to

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Quantitative Analysis of Protein ,-Acylation Site Dynamics Using Site-Specific Acyl-Biotin Exchange ABE) protocol, when combined with SILAC-based quantification, allows both the large-scale identification of palmitoylation sites and quantitative profiling of palmitoylation site changes. This approach enables palmitoylation to be studied at a systems level comparable to other more intensively studied post-translational modifications.

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Metaproteomics of Freshwater Microbial Communitiesipelines and downstream LC-MS/MS analyses. In this chapter, a semiquantitative method that spans from sample preparation to functional annotation is provided. This method has been shown to provide in-depth and representative results of both the eukaryotic and prokaryotic fractions of freshwater microbiomes.

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Experimental Design in Quantitative Proteomicsmight cause misleading findings in MS-based experiments. We also present results of an experiment aimed at investigating variability of the intensity measurements produced by a MALDI-TOF mass spectrometer. The knowledge about the potential sources of systematic and random errors is fundamental in order to properly design an MS experiment.

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Assessment of Ubiquitin Chain Topology by Targeted Mass Spectrometrys the small protein ubiquitin as a posttranslational modifier (PTM). Clinically, the modification is of great importance as its disruption is the cause of many diseases. Unlike other PTMs, ubiquitin can encode several cellular signals by being attached as a single molecule or as a chain of several u

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