Proteome Research: Mass Spectrometry (Principles and Practice)
Proteome Research: Mass Spectrometry (Principles and Practice)
Last Updated on Friday, 9 July 2010 11:13 Written by Administrator Friday, 9 July 2010 11:13
Proteome Research: Mass Spectrometry (Principles and Practice)
Recent advances in large-scale DNA sequencing technology have made it possible to sequence the entire genome of an organism. Attention is now turning to the analysis of the product of the genome, the proteome, which is the set of proteins being expressed by a cell. Two-dimensional gel electrophoresis can be used to create cellular protein maps which give a quantitative and qualitative picture of the proteome. Mass spectrometry is the method of choice for the rapid large-scale idenfification of these proteomes and their modifications. An understanding of these methods is critical for scientists in the “Post-Genome” era.
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Review – for product Proteome Research: Mass Spectrometry (Principles and Practice)
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Although the title of this book adopts the term “proteome” (no doubt to aid sales) it describes essentially mass spectrometry of peptides and proteins. After an introductory chapter by the editor, the next chapters are devoted to specific mass spectrometers, namely electrospray ionisation on triple quadrupoles and matrix-assisted laser desorption ionisation on time-of-flight instruments. Three chapters describe MS approaches to identify proteins including mass fingerprinting and sequencing with the aid of automated tandem MS/MS spectra interpretation. The analysis of post-translational modifications, in the form of phosphorylation and glycosylation, is described followed by a comprehensive chapter of protein databases. The book ends with chapter discussing instrument configurations and somewhat of a focus on FT-ICR’s. What the book lacks is an inclusion of applications in proteome analysis by mass spectrometry. This is probably because there is very little published data on the subject, while the “proposed” research has received considerable mileage. Another curious feature of this text is the selection of authors. Of particular note is the editor who tackles the chapters on protein mass fingerprinting and interpreting tandem mass spectrometry despite a lack of publications in both areas. Little wonder then section 8.2.4 spends some time discussing charge-localisation and its influence on peptide fragmentation for low energy MS/MS spectra and not high-energy collision spectra where this phenomenon is far more evident. In short, a possibly useful book if you have the dollars to spare. If not, head to your book shelf or library for one on protein mass spectrometry. There’s not much new here.