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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(TM) 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.
List of contents
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
Summary
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.
