Practical Aspects of Trapped Ion Mass Spectrometry, Volume IV: Theory and Instrumentation: 4
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Summary Reflecting the substantial increase in popularity of quadrupole ion traps and Fourier transform ion cyclotron resonance FT-ICR mass spectrometers, Practical Aspects of Trapped Ion Mass Spectrometry, Volume IV: Theory and Instrumentation explores the historical origins of the latest advances in this expanding field.
This book would be an invaluable starting point for someone interested in becoming familiar with mass spectrometry, or for chemists or biochemists who wish to obtain a broad overview of protein MS. There are few details on interpreting mass spectra, and no detailed protocols; the book concentrates on its task of painting the broad outlines of its subject, which it does very well. However, the writing style is a bit dull, contains many careless mistakes and typos, and is confusing in places.
For example, on page the author says that fast atom bombardment FAB MS is practically useless for glycoproteins because glycopeptides rarely give a signal; but 5 pages later, after a detour through ESI and MALDI, the author returns to FAB and says that it is customary to derivatize glycopeptides before FAB-MS, and that FAB-MS analysis of glycoproteins provides a wealth of information, including compositions, heterogeneity, and oligosaccharide sequences.
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Figure 9. Despite the many points of comparison of the different types of mass spectrometry throughout the book, it is not until page that the author gets around to saying that MALDI is at least 10 times more sensitive than ESI. Nonetheless, the book is highly recommended to anyone interested in understanding mass spectrometers. The book is a clear and detailed exposition of interpreting mass fragmentation spectra of proteins, concentrating exclusively on patterns created by electrospray ionization ESI.
No detail of this incredibly boring but important subject is left to the imagination. The book contains numerous examples and exercises even in the appendix , and has long chapters on interpretation of phosphoprotein spectra and glycoprotein spectra. Full of diagrams and illustrations. But if you do, there's a lot of basic stuff you need to learn fast.
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This is the book to read if you know nothing about HPLC or mass spectrometry, before you start on the operating manuals. While there's some practical information in this book, it will be mostly review for anyone with any experience with HPLC or mass spec. The comments about HPLC are useful for those running 4. Nanospray uses or micron silica capillaries, and doesn't require splitters which throw most of your sample away at the detector. Most of the suggestions in this book, like filtering your sample, simply won't work on these more modern systems, where your sample is often only a couple of microliters.
The discussion of mass spectrometers is fairly general and of limited use even for beginners. McMaster tends to drift into the uses of different types of mass spectrometry, and in so doing misses an opportunity to explain how to really maintain the mass spec. That would have made this a truly useful book. Covers droplet formation, fragmentation patterns of various types of biomolecules, and some specialized topics like nucleic acids and glycoconjugates. Too general for those with a practical problem, and too scattershot for those seeking in-depth knowledge, but a good way to get oriented to the capabilities of ESI.
While the information is presented at a fairly sophisticated level, the title is somewhat misleading. The only chapter that is of practical use to experimenters is the one on glycoprotein fragmentation. If you are, then you have to have this book. Short but useful if you just want to learn how to do it, and don't care how it works.
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Unlike Quantitative Proteomics by Mass Spectrometry , this book is not a collection of protocols--it teaches the principles you need to know for routine analysis of proteins. About half the book is dedicated to the software Sequest, homology searching, and databases. There are also chapters on identifying phosphoproteins and glycoproteins.
Very good for anyone just starting out.
Practical Aspects of Ion Trap Mass Spectrometry, Volume I
ALDI matrix-assisted laser desorption ionization is a technique that uses laser ablation of a sample-coated target to vaporize molecules for injection into a mass spectrometer. This means that fragile biomolecules such as proteins can produce a single peak without being fragmented. However, most current-generation TOF machines have a limited dynamic range. This is probably because of the great difficulty in obtaining reliable quantitative results with such machines. Even so, MALDI can be useful in molecule identification and structural studies, where accurate measurements aren't so important.
It provides a good basic understanding of the technology for researchers contemplating the use of MALDI in their experiments.