At present where protein identification and characterisation using mass spectrometry is a method of choice, this book is presenting a review of basic proteomic techniques. The second part of the book is related to the novel high throughput protein identification technique called the 'molecular scanner'.
Several protein identification techniques are described, especially the peptide mass fingerprint with MALDI-MS based method. E.g. ionisation process, matrix available, signal reproducibility and suppression effect, as well as date treatment for protein identification using bioinformatics tools.
Gives a large overview of protein/peptide chemistry developed over, at least, the last fifty years, e.g. animo or carboxylic groups modifications, charged group derivatisation and stable isotope labelling
Preface, Acknowledgements, List of Contributors, 1: Introduction: Proteins analysis using mass spectrometry; 2: Molecular scanner development: Toward clinical molecular scanner for proteome research: Parallel protein chemical processing before and during western-blot; 3: Quantitation during electroblotting step: Enhanced protein recovery after electrotransfer using square wave alternating voltage; 4: Signal traitment and virtual imaging (1/2): A molecular scanner to highly automated research and to display proteome images; 5: Signal traitment and virtual imaging (2/2): Visualization and analysis of molecular scanner peptide mass spectra; 6: Improvement in the peptide mass fingerprint protein identification (1/2): Hydrogen/deuterium exchange for higher specificity of protein identification by peptide mass fingerprinting; 7: Improvement in the peptide mass fingerprint protein identification (2/2): MALDI-MS/MS with high resolution and sensitivity for identification and characterization of proteins; 8: Proteomic and mass spectrometry: Some aspects and recent developments; 9: Conclusions and perspectives; Appendix; Abbreviations used in this book; Abbreviations for usual amino acids and chemical constants; Index.