Buch, Englisch, Band 753, 400 Seiten, Format (B × H): 187 mm x 263 mm, Gewicht: 911 g
Reihe: Methods in Molecular Biology
Methods and Protocols
Buch, Englisch, Band 753, 400 Seiten, Format (B × H): 187 mm x 263 mm, Gewicht: 911 g
Reihe: Methods in Molecular Biology
ISBN: 978-1-61779-147-5
Verlag: Humana Press
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.
Zielgruppe
Professional/practitioner
Autoren/Hrsg.
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Weitere Infos & Material
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
