De Novo Peptide Sequencing by Nanoelectrospray Tandem Mass Spectrometry Using Triple Quadrupole and Quadrupole/Time-of-Flight Instruments -- Direct Analysis of Proteins in Mixtures -- Characterization of a Mutant Recombinant S100 Protein Using Electrospray Ionization Mass Spectrometry -- Searching Sequence Databases via De Novo Peptide Sequencing by Tandem Mass Spectrometry -- Signature Peptides From Analytical Chemistry to Functional Genomics -- Investigating the Higher Order Structure of Proteins -- Probing Protein Surface Topology by Chemical Surface Labeling, Crosslinking, and Mass Spectrometry -- Secondary Structure of Peptide Ions in the Gas Phase Evaluated by MIKE Spectrometry -- Preparation and Mass Spectrometric Analysis of S-Nitrosohemoglobin -- Multiple and Subsequent MALDI-MS on-target Chemical Reactions for the Characterization of Disulfide Bonds and Primary Structures of Proteins -- Epitope Mapping by a Combination of Epitope Excision and MALDI-MS -- Identification of Active Site Residues in Glycosidases by Use of Tandem Mass Spectrometry -- Probing Protein-Protein Interactions with Mass Spectrometry -- Studies of Noncovalent Complexes in an Electrospray lonization/ Time-of-Flight Mass Spectrometer -- Kinetic Analysis of Enzymatic and Nonenzymatic Degradation of Peptides by MALDI-TOFMS -- Characterization of Protein Glycosylation by MALDI-TOFMS -- Positive and Negative Labeling of Human Proinsulin, Insulin, and C-Peptide with Stable Isotopes -- Identification of Snake Species by Toxin Mass Fingerprinting of Their Venoms -- Mass Spectrometric Characterization of the ?-Subunit of Human Chorionic Gonadotropin -- Analysis of Gluten in Foods by MALDI-TOFMS -- Quantitation of Nucleotidyl Cyclase and Cyclic Nucleotide-Sensitive Protein Kinase Activities by Fast-Atom Bombardment Mass Spectrometry -- Influence of Salts, Buffers, Detergents, Solvents, and Matrices on MALDI-MS Protein Analysis in Complex Mixtures -- Sample Preparation Techniques for Peptides and Proteins Analyzed by MALDI-MS -- Analysis of Hydrophobic Proteins and Peptides by Mass Spectrometry -- Analysis of Proteins and Peptides Directly from Biological Fluids by Immunoprecipitation/Mass Spectrometry -- Detection of Molecular Determinants in Complex Biological Systems Using MALDI-TOF Affinity Mass Spectrometry -- Rapid Identification of Bacteria Based on Spectral Patterns Using MALDI-TOFMS.

New types of mass spectrometric instrumentation and new ionization techniques have dramatically extended the applicability of mass spectrometry to the analysis of proteins and peptides. In Mass Spectrometry of Proteins and Peptides, John R. Chapman recreates the success of his earlier acclaimed book (Protein and Peptide Analysis by Mass Spectrometry, 1996) with a major new collection of cutting-edge methods in this area. Contributed by well-established investigators, each chapter provides background information before guiding the researcher step-by-step through the experimental process, with detailed instructions to help assure experimental success. The applications covered range widely and include protein sequencing, higher-order structure determination, epitope mapping, kinetics, quantitation, glycosylation analysis, and bacterial typing. Authoritative and eminently practical, Mass Spectrometry of Proteins and Peptides demonstrates the full scope of this versatile analytical technique. All protein chemists and biochemists, as well as bioanalytical scientists, who want to exploit these powerful methods in their work, will find this book indispensable.