Mass Spectrometry of Proteins and Peptides

1. Front Matter

   Pages i-xiv

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2. De Novo Peptide Sequencing by Nanoelectrospray Tandem Mass Spectrometry Using Triple Quadrupole and Quadrupole/Time-of-Flight Instruments

   • Andrej Shevchenko, Igor Chernushevich, Matthias Wilm, Matthias Mann

   Pages 1-16

3. Direct Analysis of Proteins in Mixtures

   • John R. Yates III, Andrew J. Link, David Schieltz

   Pages 17-26

4. Characterization of a Mutant Recombinant S100 Protein Using Electrospray Ionization Mass Spectrometry

   • Mark J. Raftery

   Pages 27-39

5. Searching Sequence Databases via De Novo Peptide Sequencing by Tandem Mass Spectrometry

   • Richard S. Johnson, J. Alex Taylor

   Pages 41-61

6. Signature Peptides From Analytical Chemistry to Functional Genomics

   • Haydar Karaoglu, Ian Humphery-Smith

   Pages 63-94

7. Investigating the Higher Order Structure of Proteins

   • John R. Engen, David L. Smith

   Pages 95-112

8. Probing Protein Surface Topology by Chemical Surface Labeling, Crosslinking, and Mass Spectrometry

   • Keiryn L. Bennett, Thomas Matthiesen, Peter Roepstorff

   Pages 113-131

9. Secondary Structure of Peptide Ions in the Gas Phase Evaluated by MIKE Spectrometry

   • Igor A. Kaltashov, Aiqun Li, Zoltán Szilágyi, Károly Vékey, Catherine Fenselau

   Pages 133-146

10. Preparation and Mass Spectrometric Analysis of S-Nitrosohemoglobin

    • Pasquale Ferranti, Gianfranco Mamone, Antonio Malorni

    Pages 147-165

11. Multiple and Subsequent MALDI-MS on-target Chemical Reactions for the Characterization of Disulfide Bonds and Primary Structures of Proteins

    • H. Peter Happersberger, Marcus Bantscheff, Stefanie Barbirz, Michael O. Glocker

    Pages 167-184

12. Epitope Mapping by a Combination of Epitope Excision and MALDI-MS

    • Carol E. Parker, Kenneth B. Tomer

    Pages 185-201

13. Identification of Active Site Residues in Glycosidases by Use of Tandem Mass Spectrometry

    • David J. Vocadlo, Stephen G. Withers

    Pages 203-222

14. Probing Protein-Protein Interactions with Mass Spectrometry

    • Richard W. Kriwacki, Gary Siuzdak

    Pages 223-238

15. Studies of Noncovalent Complexes in an Electrospray lonization/ Time-of-Flight Mass Spectrometer

    • Andrew N. Krutchinsky, Ayeda Ayed, Lynda J. Donald, Werner Ens, Harry W. Duckworth, Kenneth G. Standing

    Pages 239-249

16. Kinetic Analysis of Enzymatic and Nonenzymatic Degradation of Peptides by MALDI-TOFMS

    • Fred Rosche, Jörn Schmidt, Torsten Hoffmann, Robert P. Pauly, Christopher H.S. McIntosh, Raymond A. Pederson et al.

    Pages 251-272

17. Characterization of Protein Glycosylation by MALDI-TOFMS

    • Ekaterina Mirgorodskaya, Thomas N. Krogh, Peter Roepstorff

    Pages 273-292

18. Positive and Negative Labeling of Human Proinsulin, Insulin, and C-Peptide with Stable Isotopes

    • Reto Stöcklin, Jean-François Arrighi, Khan Van Hoang-, Lan Vu, Fabrice Cerini, Nicolas Gilles et al.

    Pages 293-315

19. Identification of Snake Species by Toxin Mass Fingerprinting of Their Venoms

    • Reto Stöcklin, Dietrich Mebs, Jean-Claude Boulain, Pierre-Alain Panchaud, Henri Virelizier, Cécile Gillard-Factor

    Pages 317-335

20. Mass Spectrometric Characterization of the β-Subunit of Human Chorionic Gonadotropin

    • Roderick S. Black, Larry D. Bowers

    Pages 337-354

Little more than three years down the line and I am already writing the Preface to a second volume to follow Protein and Peptide Analysis by Mass . What has happened in between these times to make this second venture worthwhile? New types of mass spectrometric instrumentation have appeared so that new techniques have become possible and existing techniques have become much more feasible. More particularly, however, the newer ionization te- niques, introduced for the analysis of high molecular weight materials, have now been thoroughly used and studied. As a result, there has been an en- mous improvement in the associated sample handling technology so that these methods are now routinely applied to much smaller sample amounts as well as to more intractable samples. Again, this particular community of mass spectrometry users has both increased in number and diversified. And, riding this wave of acceptance, leaders in the field have set their sights on more complex problems: molecular interaction, ion structures, quantitation, and kinetics are just a few of the newer areas reported in Mass Spectrometry of Proteins and Peptides. As with the first volume, one purpose of this collection, Mass Spectr- etry of Proteins and Peptides, is to show the reader what can be done by the application of mass spectrometry, and perhaps even to encourage the reader to venture down new paths.

"John Chapman has followed on from his excellent earlier volume 'Protein and Peptide Analysis by Mass Spectrometry' by bringing together in this both very readable and informative volume 27 individual chapters from acknowledged practitioners of the application of mass spectrometry to peptides and proteins. Each chapter is packed with real information both for the biologist and mass spectroscopist and contains a wealth of detail on sample reparation and the subsequent interpretation of the MS results. ...The 'hot' topics of the investigation of non-covalent complexes, protein-protein interactions and higher order protein structures by mass spectrometry are addressed in separate chapters. Any laboratory working on peptides and proteins whether they use MS or not should have access to this book. It is a goldmine."-European Peptide Society Newsletter

"...a well crafted book using the experience of respected pioneers of modern mass spectrometric methods....Many of the methods used in proteomic studies rely on mass spectrometric analysis of proteins and peptides, as well as protein separation technology. The latter is dealt with to some extent by this volume; however, the mass spectrometric aspects are very well covered....This volume shows the great versatility of mass spectrometric analysis, in this case related to protein and peptides, indicating that most analytical challenges can be met by the technique, especially when combined with innovative sample preparation. For the clinical biochemist with an interest in proteins and peptides, this volume is an important reference. For other biochemists it represents a view of a great potential, which will develop as our use of the human genome information progresses."-Annals of Clinical Biochemistry

"The availability of a compilation of authoritative reviews that include a wealth of practical detail regarding sample preparation and presentation as well as instrument operation is both timely and of considerable value. In total there are some twenty-seven comprehensive descriptions of mass spectrometric analyses of proteins, peptides and mixtures of various complexity and provenance. The elucidation of higher-order structure is described as well as primary sequence determination, epitope mapping and cell typing using several substrates from highly refined isolates to more complex mixtures and whole cells. The contributions are provided by over sixty well established researchers and include detailed information for sample isolation and preparation as well as a comprehensive bibliography on each topic area. Further information is collated into a series of appendices covering an abbreviation glossary, listings of mass/abundance values for elements, amino acids and monosaccharide residues and a literature update on protein mass spectrometry for 1997 - 1998. This volume is a valuable addition to the series: it is comprehensive in terms of the range of applications considered and extensive in the descriptions of the analytical process. It is unusual among reviews of mass spectrometric applications for the wealth of experimental detail provided an this aspect alone makes it an essential item for every biological mass spectrometry and proteomics laboratory." - Chromatographia

• Sale, Manchester, UK

  John R. Chapman

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