Proteomic Profiling and Analytical Chemistry

Preface
1. Introduction
Jerzy Silberring and Pawel Ciborowski
2. Biomolecules
Ariel Burns, Pawel Olszowy and Pawel Ciborowski
3. General Strategies for Proteomic Sample Preparation
Piotr Suder, Peter Novak, Vladimir Havlicek and Anna Bodzon-Kulakowska
4. Protein Extraction and Precipitation
Petr Novak and Vladimir Havlicek
5. Online and Offline Sample Fractionation
Marek Smoluch, Przemyslaw Mielczarek, Anna Drabik and Jerzy Silberring
6. Immunoaffinity Depletion of High-Abundant Proteins for Proteomic Sample Preparation
Jayme Wiederin and Pawel Ciborowski
7. Gel Electrophoresis
Anna Drabik, Anna Bodzon-Kulakowska and Jerzy Silberring
8. Quantitative Measurements in Proteomics: Mass Spectrometry
Anna Drabik and Jerzy Silberring
9. SWATH-MS: Data Acquisition and Analysis
Kristin Frederick and Pawel Ciborowski
10. Top-Down Proteomics
Cory Boone and Jiri Adamec
11. Proteomic Database Search and Analytical Quantification for Mass Spectrometry
Melinda Wojtkiewicz, Jayme Wiederin and Pawel Ciborowski
12. Design and Statistical Analysis of Mass-Spectrometry-Based Quantitative Proteomics Data
Fang Yu, Fang Qiu and Jane Meza
13: Principles of Analytical Validation
Jo-Ellyn McMillan
14.Validation in Proteomics and Regulatory Affairs
Jerzy Silberring, Melinda Wojtkiewicz and Pawel Ciborowski

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• Química analítica
• Proteinas

Absolute quantitation; Accuracy; Agarose gel electrophoresis; Albuminome; Analytical chemistry; Analytical quantification; Analytical validation; Bioinformatics; Calibration curve; Capillary columns; Capillary isoelectric focusing; Cerebrospinal fluid protein extraction; Chromatographic techniques; Clustering; Coomassie Brilliant Blue; Cross-validation; Crude protein extraction; C-terminal labeling; Cysteine and methionine; Data analysis; Database search; Data-dependent acquisition; Data-independent acquisition; Design; Detection level; Detergents; Difference gel electrophoresis; False-discovery rate; Fluorescent staining; Gel electrophoresis; Gel-based quantitative proteomics; Homogenization; Hydropathy index; Hydrophilic interaction liquid chromatography; Hydrophilicity; Hydrophobic interaction chromatography; Hydrophobic proteins; Hydrophobicity; Immunoaffinity; Immunodepletion; Instrument validation; Internal standard; Ion exchange chromatography; Ion-exchange chromatography; Isoelectric focusing; Isoelectric point precipitation; Isotope labeling; Isotope-coded affinity tagging; Label-free quantification; Lipids; Liquid chromatography; Mass spectrometry data searches; Mass spectrometry; Method validation; Monolith; Native polyacrylamide electrophoresis; N-terminal labeling; Offline fractionation; One-dimensional electrophoresis; Online fractionation; Organic solvent-driven precipitation; Peptide purification; Post-database search data processing; Precision; Prefractionation; Protease inhibitors; Protein databases; Protein extraction; Protein folding; Protein moonlighting; Protein precipitation; Protein separation; Proteomic sample preparation; Proteomic samples; Proteomics; Quantitative proteomics; Randomization; Recovery; Regulation; Relative quantitation; Replication; Reproducibility; Reversed-phase liquid chromatography; Salting out; Sample loss; Sample size calculation; SDS-PAGE; Search engines; Selectivity; Serum protein extraction; Size-exclusion chromatography; Size-exclusion filters; Specificity; Spectral library; Stability; Stable isotope labeling; Statistical analysis; Strong cation exchanger; SWATH-MS; Top-down proteomics; Trichloroacetic acid precipitation; Two-dimensional electrophoresis; Validation; z-score transformation