Guided tour of body's dreamy spires

It is thrilling to read a book that excites with both the way it presents the available information and the elegance with which this information is analysed. Such a book is Introduction to Protein Architecture by Arthur Lesk. At the outset, he introduces the reader to the main features exhibited by the wonderful structure of the photo-reaction centre and displays the images in beautiful stereoscopic views. I do not see how any nascent scientist could fail to be interested in such an introduction to a challenging subject. Thereafter, the book comes down to earth, but gently, so that one is encouraged to read on into the delights of "protein folding" and "methods of structure determination".

Thank goodness that the author emphasises the strength of the worldwide web since many books will, in future, be necessary and extremely valuable adjuncts of visits to the web, "webenquiries". Lesk lists many websites throughout, and those I visited were most interesting and useful. Likewise, the references are well chosen and the problems and "weblems" fascinating.

It was most encouraging to read the author's opinion of structure determination by NMR spectroscopy in comparison with that by X-ray crystallography. Obviously, the latter is more commonly used but to detail the weaknesses and strengths of each is a sign of the increasing maturity of the former, at least as far as investigations of relatively small biomolecules is concerned. It is remarkable to realise that some 10,000 protein structures are known, though if current plans come to fruition, this number may increase by at least 1,000 a year.

The chapters on molecular evolution and on conformational changes in proteins are particularly strong. In the latter, although the author discusses, at some length, movement within structure, he barely touches on current attempts to derive information, using the synchrotron source, to investigate kinetic phenomena. I would have liked to see a small section on the structures of viruses and would have preferred some discussion of how we might infer from the structures of individual proteins their interaction in concert in the cell. That said, I heartily recommend this book (which, by the way, is beautifully produced) to any reader, young or old, who chances upon it. Indeed, it must not be left to chance but should be recommended reading for all those physical or biological scientists who are excited by sheer elegance.

H. Allen O. Hill is professor of bioinorganic chemistry, University of Oxford.