92 BioEssays Vol. 8, No. 2 - FebruaryIMarch 1988

Protein Engineering Protein Engineering : Applications in Science, Medicine and Industry. Edited by M. Inouge and R. Sarma, Academic Press, Orlando, Fla, 1986. Pp. 440. $49.95. By Alan Russell The term ‘protein engineering’ has become widely used, and now it gener- ally refers to the systematic replacement of amino acid residues by other residues in order to alter the properties of a protein. There are a vast number of workers using the techniques of site- directed mutagenesis to alter and study protein structure and function. With this in mind it would be almost impos- sible to bring together in one volume all of the important work in the field: especially if one broadens the meaning of protein engineering to include any technique which will alter the function of a protein. Thus, it is not surprising that this book falls far short of being such a comprehensive treatise. Rather, the book is a useful collection of results, discussions and conclusions (mostly from a recent conference) for those already working in the field. It is especially noticeable that the book contains no references to the exciting work on tyrosyl tRNA synthetase which many would argue is the father of the subject.

There is still, however, much exciting work described in the book, and it is unfortunate that there is not enough space to discuss the work of all eighty- six contributing authors. The book is split into four sections: Structure and Design; Mutant Analysis; Complex Systems ; Applications. Since the editors offer no summary of the contributions and since there is considerable overlap between the sections, the book seems disjointed and for that reason hard to follow.

One of the major goals of protein engineering is to create more thermo- stable proteins. The book contains two chapters which address this problem. The first, by Oshima, considers the structure and function of proteins which are already thermostable, in the hope that a detailed investigation will give clues as to why one protein is more thermostable than another. Later in the book Wetzel describes how he has used the approach of introducing disulphide bonds to increase thermostability. Although the mutant protein shows increased thermostability to reversible

inactivation, the use of this method has not been successful for other proteins, and much is still to be learnt about the process of thermoinactivation itself.

Kaiser (chapter 5) and Atassi (chapter 9) both describe how it has been possible to design small peptides which will mimic the properties of a part of a protein. These types of investigation into molecular recognition are of funda- mental importance and will form part of the database necessary for the ulti- mate goal of ab initio protein design.

The book closes with a section on the ‘Applications ’ of protein engineering. A particularly interesting chapter is written by Klibanov on the use of enzymes in organic solvents. This has led to the discovery that enzymes are stable at very high temperatures, can perform novel reactions, and yet retain specificity when placed in organic sol- vents with essentially no water. This novel, extremely successful, and little- understood approach to altering the functionality of proteins has yielded a whole new area of research. This will not fit into our present definition of protein engineering, and perhaps before too long we will see books on ‘solvent engineering ’ .

To summarize, the book is essentially a collection of articles by some of the workers in the field, and as such is probably not suitable for those just entering the subject. The book provides a very useful database for those active in the broad field of protein engineering, particularly if the reader is looking for review-type articles by leading authors.

ALAN J. R U S S E L L is at the Department of Applied Biological Sciences, Rm 16-215, Massachusetts Institute of Technology, Cambridge M A 02139, USA.

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Reviews of M a crom o I ec u I a r Structure: A Needed Compendium? Protein and Nucleic Acid Structure and Dynamics, Edited by J. KING, Annual Reviews Special Collections Pro- gramme. Benjamin/Cummings. 1985. Pp. 587. €29.95. By E. James Milner-White This book is a compendium of articles taken from Annual Reviews of Biochem- istry (ARB) 1980-4. Some of the articles are good but it is not obvious why

anybody should want to buy it. Those working in the area will have read some of the articles already, as ARB is in most libraries. On the other hand, for anyone not familiar with this subject, this book is not the place to start.

I peruse ARB regularly. It also serves a useful role as somewhere to start for the purpose of looking up recent refer- ences on any subject. However, it is rather indigestible; it suffers from a shortage of diagrams and pictures ; and it rapidly goes out of date. At worst, a review in ARB consists entirely of a list of references to the work done in the area since the last ARB review was written; it alludes to, but does not actually describe, the work that has been done, or, if described, the con- clusions are ambiguous. Although an exaggeration, this does apply to some of the articles in the book. The lack of diagrams applies too ; the reviews on myosin, on DNA chemistry and on protein NMR have none, while those on DNA structure (how can you de- scribe propeller twist without a dia- gram?), protein-folding intermediates and nucleosomes have few. Even the front cover is a disappointment, being a black and white picture of Bob Lan- gridge’s dot surface picture of the trypsin-trypsin inhibitor complex, just like the one, in colour, on the cover of Lehninger’s Biochemistry. This now over-used picture is almost meaningless without colour. With regard to being out of date, the nature of this type of review, especially in a fast-moving field such as this, is that it rapidly becomes outmoded. For example, there is no mention of the histidinesysteine-zinc DNA-binding finger domains in the section on protein-DNA recognition.

Half of the book is devoted to proteins, half to nucleic acids and protein-nucleic acid recognition. In the protein section there are good reviews on folding (Rossmann & Argos and Chothia), polypeptide hormones (Blun- dell & Wood), folding intermediates (Kim & Baldwin), dynamics (Karplus & McCann) and membrane proteins (Eisenberg). I would have replaced the chapter on myosin, which is misplaced, by a review on an enzyme that has been studied in detail by X-ray crystallo- graphy. In the nucleic acids section, the reviews on Z-DNA (Rich et a,.) and protein-DNA recognition (Pabo & Sauer) are enjoyable, but the problem of being outdated is even more acute. The chapters on snRNAs and nu-