Proteomic Profiling and Analytical Chemistry : the Crossroads
Proteomic Profiling and Analytical Chemistry helps scientists without a strong background in analytical chemistry to understand basic analytical principles and apply them to proteomics profiling. In most proteomic profiling experiments, liquid chromatography is used; this method is also used widely in analytical chemistry. This book bridges the gap between overly specialized courses and books in mass spectrometry, proteomics and analytical chemistry. It also helps researchers with an analytical chemistry background to break into the proteomics field. Proteomic Profiling and
1 online resource (259 pages)
9780444593788, 9781283941532, 9780444593917, 0444593780, 1283941538, 0444593918
1058399494
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Front Cover; Proteomic Profiling and Analytical Chemistry: The Crossroads; Copyright; Contents; Preface; CHAPTER 1
INTRODUCTION; 1.1 Why Analytics Matter?; 1.2 Expectations: Who and What?; 1.3 What Is Next and Where Are We Going?; CHAPTER 2
BIOMOLECULES; 2.1 Major Features and Characteristics of Proteins and Peptides; 2.2 Hydrophilicity and Hydrophobicity; 2.3 Effect of Protein Fragmentation; 2.4 Effect of Post-translational Modifications; 2.5 Amino Acid Sequence and Separating Conditions; 2.6 Cysteine and Methionine; Amino Acids Containing Sulfur. 2.7 Protein Identification and Characterization2.8 Structure-Function Relationship and Its Significance in Systems Biology Function; 2.9 Protein Folding and Protein-Protein Interactions; 2.10 Moonlighting of Proteins; References; CHAPTER 3
FUNDAMENTAL STRATEGIES OF PROTEIN AND PEPTIDE SAMPLE PREPARATION; SECTION 3.1
GENERAL STRATEGIES FOR PROTEOMIC SAMPLE FRACTIONATION; 3.1.1 Introduction; 3.1.2 Inhibition of Protease Activity; 3.1.3 Homogenization; 3.1.4 Cells as Source of Biological Material for Proteomics; 3.1.5 Subcellular Compartments: Organellar Proteomics. 3.1.6 Crude Protein Extract: What Is the Next Step?3.1.7 Fractionation Based on Size-Exclusion Filters; 3.1.8 Chromatographic Methods of Protein Fractionation; 3.1.9 Peptide Purification; 3.1.10 Summary; Acknowledgments; References; SECTION 3.2
CAPILLARY COLUMNS FOR PROTEOMIC ANALYSES; 3.2.1 Introduction; 3.2.2 Conventional Capillary Columns; 3.2.3 Monolithic Columns; 3.2.4 Summary and Conclusions; References; SECTION 3.3
ION-EXCHANGE CHROMATOGRAPHY; 3.3.1 Historical Perspective; 3.3.2 Principle of Ion-Exchange Chromatography; 3.3.3 Common Types of IEC Stationary Phases. 3.3.4 Choice of Ion Exchanger (Cation or Anion?)3.3.5 Choice of Strong or Weak Ion Exchanger; 3.3.6 Buffers in IEC; 3.3.7 Ion-Exchange Chromatography in Proteomic Studies; References; CHAPTER 3.4
PROTEIN AND PEPTIDE SEPARATION BASED ON ISOELECTRIC POINT; 3.4.1 Principles of Isoelectric Focusing (IEF); 3.4.2 Sample Preparation Prior to IEF; 3.4.3 Isoelectric Focusing in Liquid State; 3.4.4 Immobilized pH gradient IEF; 3.4.5 Capillary IEF (CIEF); 3.4.6 Isoelectric Focusing in Living Organisms; 3.4.6 Summary; References; CHAPTER 4
PROTEIN EXTRACTION AND PRECIPITATION; 4.1 Introduction. 4.2 Inhibitors of Proteolytic and Other Enzymes4.3 Focus on Hydrophobic Protein Extraction; 4.4 On the Role of Protein Solvation; 4.5 Protein Precipitation; 4.6 Salting Out; 4.7 Isoelectric Point Precipitation; 4.8 Organic Solvent-Driven Precipitation; 4.9 Trichloroacetic Acid Precipitation; 4.10 Detergents, Lipids, and Final Remarks; References; CHAPTER 5
IMMUNOAFFINITY DEPLETION OF HIGH-ABUNDANT PROTEINS FOR PROTEOMIC SAMPLE PREPARATION; 5.1 Capacity of Immunodepletion Columns and Other Devices; 5.2 Reproducibility; 5.3 Quality Control of Immunodepletion; 5.4 Albuminome; 5.5 Summary
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