Gel-Free Proteomics

Focusing on differential analysis and protein modifications, Gel-Free Proteomics addresses contemporary methods for gel-free proteome research. The text describes the vital procedures needed to perform gel-free proteomics.

Proteomics by means of mass spectrometry has rapidly changed the way that we analyze proteomes. Gel-Free Proteomics: Methods and Protocols addresses contemporary methods for gel-free proteome research with a special focus on differential analysis and protein modifications. Divided into twenty-five chapters, this detailed volume meticulously describes vital procedures needed to perform gel-free proteomics, ranging from sample preparation, isotope labeling for differential proteomics, enrichment technologies for modified proteins and peptides, and bioinformatics. Written in the successful Methods in Molecular Biology™ series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible protocols, and notes on troubleshooting and avoiding known pitfalls. Authoritative and easily accessible, Gel-Free Proteomics: Methods and Protocols serves as a timely resource for both professionals and novices pursing research in this critical field.

Includes cutting-edge methods and protocols Provides step-by-step detail essential for reproducible results Contains key notes and implementation advice from the experts Includes supplementary material: sn.pub/extras

Inhalt
Mass Spectrometry-driven Proteomics: An Introduction .- Metabolic Labeling of Model Organisms using Heavy Nitrogen (15N) .- Trypsin-catalyzed Oxygen-18 Labeling for Quantitative Proteomics .- ICPL Labeling Strategies for Proteome Research .- Quantitative Proteome Analysis using Isobaric Peptide Termini Labeling (IPTL) .- Complete Chemical Modification of Amine and Acid Functional Groups of Peptides and Small Proteins .- Production and Use of Stable-isotope-labeled Proteins for Absolute Quantitative Proteomics .- Organelle Proteomics .- Membrane Protein Digestion Comparison of LPI Hexalane with Traditional Techniques .- GeLCMS for In-depth Protein Characterization and Advanced Analysis of Proteomes .- Exploring New Proteome Space: Combining Lys-N Proteolytic Digestion and Strong Cation Exchange (SCX) Separation in Peptide Centric MS-driven Proteomics .- Quantitation of Newly Synthesized Proteins by Pulse-labeling with Azidohomoalanine .- Analytical Strategies in Mass Spectrometry Based Phosphoproteomics .- A Protocol on the Use of Titanium Dioxide Chromatography for Phosphoproteomics .- Positional Proteomis at the N-terminus as a Means of Proteome Simplification .- N-terminomics: A High-content Screen for Protease Substrates and their Cleavage Sites .- Protease Specificity Profiling by Tandem Mass Spectrometry Using Proteome-derived Peptide Libraries .- Identification of Proteolytic Products and Natural Protein N-termini by Terminal Amine Isotopic Labeling of Substrates (TAILS) .- Lectins as Tools to Select for Glycosylated Proteins .- Strong Cation Exchange Chromatography for Analysis of Sialylated Glycopeptides .- Titanium Dioxide Enrichment of Sialic Acid-containing Glycopeptides .- Chemical de-O-Glycosylation of Glycoproteins for Applications in LC-based Proteomics .- Ubiquitination and Degradation ofProteins .- Bioinformatics Challenges in Mass Spectrometry Driven Proteomics .- A Case Study on the Comparison of Different Software Tools for Automated Quantification of Peptides

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