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Chromatographia

, Volume 65, Issue 3–4, pp 257–258 | Cite as

Book Reviews

Book Reviews
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1 How to Write a Successful Scientific Thesis: The Concise Guide For Students

1.1 by W.E.Russey, H.F.Ebel, C.Bliefert Wiley-VCH Weinheim, Germany, 2006 Pp 223. ISBN-13: 978-3-527-31298-6 Price: EUR 22.90

This is the “prequel” to the book written in 1987 by the same authors entitled “The Art of Scientific Writing”. There may be overlap between the two but I am unable to decide how much since I donated my copy of the earlier volume to a deserving home some time ago.

The format of this volume is somewhat unusual in that each chapter has a preliminary paragraph or two that state the specific aim(s) and a list of “Qs” or questions. For example Chapter 10 on the introduction to a thesis lists six questions starting with “What must one include in the Introduction”, through “What should the reader learn by perusing your Introduction”, to “What does the Introduction have in common with a review article in the published literature”? The contents of the chapter then go on to discuss these and other points at length. The body of the text is indented and the left margin contains a sort of running index with headings such as “General guidelines” and “The first person form as opposed to the traditional passive voice”. These topics are marked in the indented space as, in this particular case, Ex 10.1, and Ex.10.7. At the end of each chapter there is a list of “Cs” for Challenges or questions; the answers are given in a 20-page section at the end of the book.

The chapters follow a logical sequence from the raw data (The Laboratory Notebook) through Discussion, Results and Conclusions although I was puzzled as to why the authors place the Experimental section after Results and Conclusions—if the experimental work is considered unsatisfactory for any reason then it is a waste of time to proceed further. Apart from this, it would be difficult to criticise any of the content of these chapters, much of which is commonsense. After these chapters there are six extremely useful chapters, more about style than substance, on bibliography, appendices, footnotes, units, mathematical equations and tables. I was a little surprised to find that the authors still accept units such as mg/L since my understanding was that the recommended form is now mg L−1.

At one point, the authors state that it is a good idea to get someone, not intimately involved with the topic to check the final text. The importance of this is illustrated on page 28 where the authors refer to “.....the sample text in Ex 1–12b”, which should in fact be “....in Ex 1.13b”. The topic of jargon is not discussed and in general this text is free of jargon although I have never come across the word “factoid” on page 90, which I took from the context to mean a small fact. There is a small section on abbreviations, which states that common abbreviations such as IR, NMR and DNA are considered permissible. However, IR-MS can stand for infrared spectrometry coupled to mass spectrometry or isotope ratio mass spectrometry. Apart from this, abbreviations can quickly become tedious to a reader not totally immersed in the subject, even if they are in everyday use in the author’s lab. There is also no mention on over-reliance on the spell check facility of PCs. This is a useful facility but it should be borne in mind that the spell check program cannot distinguish between homonyms like “led” and “lead” (Pb). In my experience it will not be long now before “lead” is the accepted past participle of the verb “to lead”. This leads! me on to my final point that, although this is an excellent book which all students should read (not just post -graduates), in some ways it is a sad reflection on the standard of writing taught in the English-speaking world and especially in the UK, that such a text should be considered necessary.

E.R.Adlard

2 NMR Spectroscopy of Biological Solids

2.1 by A. Ramamoorthy (ed) CRC, Taylor & Francis, Boca Raton, FL, USA, 2006. pp. 368. ISBN 1-57444-4964-4 Price: USD 139.95, GBP 79.99

This book provides a critical review of the state-of-the-art of the rather specialised subject of solid-state NMR spectroscopy of macromolecules and is written by experts who are active in the field of research. It is a book aimed at the expert scientist who wishes to find out exactly how far this complex subject has got. It will not provide an easy introduction to the methods nor provide details of practical aspects of the studies. For example Chapter 1 jumps straight into a complex subject called dipolar recoupling. However, if one is already working in the field then this could be a valuable source of knowledge for methods and applications. Most of the biological solids as used in the title are proteins with some coverage of peptides, nucleic acids and phospholipid membranes, but nothing on complex carbohydrates.

The first few chapters describe the use of magic-angle-spinning (MAS) NMR spectroscopy. This technique involves spinning the sample rapidly at an angle of 54.7° to the magnetic field and this has the effect of removing or reducing many of the anisotropic line-broadening mechanisms that make solid state NMR so difficult. Chapter 1 is concerned with the measurement of accurate internuclear distances in solid proteins and peptides and jumps straight into detailed coverage of the methods and applications; it might have been useful to have a more introductory overview chapter at the start. The next chapter explains how MAS NMR spectra can be used to make peak assignments in NMR spectra of solid proteins, particularly those that are membrane bound and cannot be crystallised for X-ray diffraction structural studies. Chapter 3 extends the applications to cover uniformly labelled proteins and protein assemblies and shows how to obtain information on protein secondary structure. The NMR techniques used for determining bond torsional angles in proteins are reviewed in Chapter 4, covering both non-spinning and MAS methods.

Chapter 5 is more specialised, describing studies on peptides bound to biomaterial surfaces using a technique called double-quantum NMR. One of the major problems with NMR of macromolecules in the solid state is the rather broad line widths compared to solution state and hence compromised signal to noise ratios. Experimental NMR methods that try to overcome this problem are given in Chapter 6 showing that low sensitivity nuclei such as 15N can be detected via 1H NMR signals (so-called inverse detection).

Several chapters cover the study of macromolecules aligned with the NMR magnetic field. This is achieved by incorporating them into “bicelles”—bilayer micelles which, because of their macroscopic magnetic susceptibility, have a small but finite net alignment. As described in Chapter 7, concerned with membrane proteins inside bilayer micelles, appropriate measurements then yield information on anisotropic NMR parameters giving additional structural information. Chapter 8 extends this to one important family of proteins and Chapter 9 describes the use of 19F NMR spectroscopy of solid peptides. Chapter 10 covers applications to magnetically aligned phospholipid bilayers.

Chapters 11 and 12 are more theoretical in approach covering computational aspects for protein structure determination, design of NMR pulse sequences and calculation of chemical shielding tensors.

In general, the reference citations are comprehensive and allow the reader to go back to the original literature. The content is provided in such a manner that it will not go quickly out of date but will be of relevance for some considerable time. In summary, this text is meant for experts in the field and those who have detailed knowledge of NMR theory, but it provides a valuable source of information on methods and applications for all those interested either in solid state NMR techniques or structural and dynamic aspects of solid state macromolecules and their complexes.

J. Lindon

Copyright information

© Friedr. Vieweg & Sohn Verlag/GWV Fachverlage GmbH 2007

Authors and Affiliations

  1. 1.WiesbadenGermany

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