TIBS 21 - MARCH 1996

to me. Even the authors themselves specifically avoided discussing genetically engineered baculovirus pesticides and confined the discussion to naturally occurring baculoviruses.

Some of the 'applications' chapters also seemed to be too specific to be of general use. For example, DeBanne, Pacheco-Oliver and O'Connor-McCourt provide a detailed account of the large

scale purification of the extracellular domain of the epidermal growth factor receptor from baculovirus infected cells. While this will be of interest to researchers studying this receptor, 1 doubt that most other readers will find it useful.

On the whole then, the book provides a fairly comprehensive coverage of the methodology required for the generation

B00K REVIEWS of baculovirus expression vectors, and includes a certain amount of new and useful information. I expect it will find a niche on the shelves of many laboratories working with the system.

DAVID R. O'REILLY

Department of Biology, Imperial College of Science, Technology and Medicine, Prince Consort Road, London, UK SW72BB.

NMR spectroscopy for all

An NMR Primer for Life Scientists

by Henry Rattle, Partnership Press, 1995. s (124 pages) ISBN 0 9516436 3 0

The last few years have seen the emergence of nuclear magnetic resonance (NMR) spectroscopy from the backwaters of highly specialized journals to the mainstream of molecular biology research. The advances have been dramatic; seven years ago the topology, but perhaps not the detailed structure, of a protein domain, could be described with confidence. Recently, we have seen the publication of, among many other structures of equivalent complexity, the detailed structure of the SRY and LEF-1 DNA-binding domains bound to their targets. NMR is a research tool of great potential but, in practice, the elegance and utility of the technique has, for the uninitiated, been obscured by a panoply of jargon that renders many important contributions all but inaccessible to any but the inner circle of practitioners. This is unfortunate because the increasing power and rapidly evolving sophistication of NMR spectroscopy make it, in many cases, the technique of choice for determining the structure and, more especially, the dynamic properties of the smaller biological macromolecules. It is, therefore, a volume whose aim is to make NMR comprehensible to both undergraduate and postgraduate students

of biology (of any age) and is a particularly welcome addition.

What should we expect of such a book? There should be a simple and accurate explanation of the fundamental principles coupled with examples of the practice of the technique in its various applications. In addition, the expanding horizons of the subject should be treated with an eye to the future. First, the book by Henry Rattle is well on target. The principles are clearly and logically set out, the author proceeding by small steps from the fundamental physics to the output of three- and four-dimensional spectra. Second, and equally important, the encryption of different protocols - under such acronyms as HOHAHA, which add colour but little enlightenment to biologists listening to an NMR seminar - is well countered by appropriate indexing and translation.

One technique complementary to NMR spectroscopy is crystallography. Its strength is the ability to provide exquisitely detailed snapshots of precise contacts both within and between biological macromolecules. Yet these beautiful pictures might mislead in the sense that crystals provide little or no information on the dynamics of the interactions involved. Unfortunately, it is precisely these dynamic properties that determine, to a large extent, the properties of biological systems. It is here that NMR spectroscopy has a unique rote. Consequently, I was somewhat disappointed to see that the author had, for possibly understandable reasons, eschewed extensive discussion of this topic. Although at present the literature

on the application of NMR techniques to structural dynamics is limited, current developments suggest that in future this will be a growth area. In this context, more discussion of the methods of assessing internal motions using the order parameter would have been welcome. Similarly, a word on the significance of TJT 2 ratios in relation to the isotropy of tumbling would not have been out of place. I would encourage the author to provide more comprehensive coverage of these topics in future editions.

For the aficionados of chromosomal proteins, the book provides unexpected and candid insights into the origins of scientific controversy. Two years ago, the publication of two differing structures of a particular protein domain, a DNA-binding motif from the mammalian chromosomal protein HMG 1, generated some local turbulence. Henry Rattle's book takes the determination of one of these two structures as a case history, clarifying its evolution from original form through to current incarnation, thereby resolving the initial disparity.

This book is a valuable and timely volume and one that I have found both useful and illuminating. I would recommend it to all biologists who are contemplating the use of NMR spectroscopy or who have even already consigned some of their precious protein to the local NMR tube. NMR definitely deserves a wider audience.

ANDREW TRAVERS

MRC Laboratory of Molecular Biology, Hills Road, Cambridge, UK CB22QH.

Erra tum

In the January 1996 issue of TiBS, we published the Review article 'Ornithine decarboxylase antizyme: a novel type of regulatory protein' by S. Hayashi, Y. Murakami and S. Matsufuji (TiBS 21, 27-30) . Unfortunately, a number of errors have been noted. In the f irst line of the summary, it was stated that 'Antizyme plays an important role in the synthesis of ornithine decarboxylase...'. This sentence should read 'Antizyme plays an important role in the degradation of ornithine decarboxylase...'.

In addition, on page 29, reference citations 33 and 32, under the subheading of 'Antizyme functional domain', have been accidentally transposed.

We apologise to the authors and to our readers for these mistakes.

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