publication info
J. Chapman, ed., Humana Press, 2000, 539 pp., hard cover
General description
This new collection of cutting-edge methods in analyzing proteins and peptides is a revision of the acclaimed 1996 book. Each chapter provides background information before guiding a researcher step-by-step through the experimental process, with detailed instructions to help assure experimental success. Applications covered include protein sequencing, higher-order structure determination, epitope mapping, kinetics, quantitation, glycosylation analysis, and bacterial typing.
Table of Contents
De Novo Peptide Sequencing by Nanoelectrospray Tandem Mass Spectrometry Using Triple Quadrupole and Quadrupole/ Time-of-Flight Instruments,
Direct Analysis of Proteins in Mixtures: Application to Protein Complexes,
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: Hydrogen Exchange, Proteolytic Fragmentation, and Mass Spectrometry,
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: Relevance to Native Conformations,
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 Ionization/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: New Tools for In Vivo Pharmacokinetic and Metabolic Studies,
Identification of Snake Species by Toxin Mass Fingerprinting of Their Venoms.
Mass Spectrometric Characterization of the b-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: A Paradigm for Multiple Component Monitoring in Enzyme Incubations by Quantitative 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,
Appendices, Index.
Direct Analysis of Proteins in Mixtures: Application to Protein Complexes,
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: Hydrogen Exchange, Proteolytic Fragmentation, and Mass Spectrometry,
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: Relevance to Native Conformations,
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 Ionization/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: New Tools for In Vivo Pharmacokinetic and Metabolic Studies,
Identification of Snake Species by Toxin Mass Fingerprinting of Their Venoms.
Mass Spectrometric Characterization of the b-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: A Paradigm for Multiple Component Monitoring in Enzyme Incubations by Quantitative 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,
Appendices, Index.
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