The first of the six chapters covers the covalent structures of peptides and proteins, starting with the 20 translational amino acids and their stereochemistry, and going on to the acid/base and hydrophobic/hydrophilic properties of their side chains. The peptide bond, and the composition and electrical properties of peptides are then discussed. This is a good introduction although I feel that some discussion of the biological synthesis of proteins, including transcription, translation and post-translational modification might have been included without unduly affecting the length of the chapter. This would have shown the relevance of the 20 translational amino acids and yet indicated that biologically important proteins can contain many more amino acids than these. Chapter 2 describes the chemical synthesis of peptides and introduces the reader to the concepts of protection, coupling and to the dangers of racemisation in synthesis. It also describes the solution and solid phase approaches and stresses the importance of purifying and characterising the final product. I was somewhat surprised that the excellent Oxford primer on amino acid and peptide synthesis by John Jones was not included among the suggestions for further reading.
Chapter 3 deals with the particular problems encountered in purification of proteins and I found this an extremely valuable account for the beginner in the protein field. Chapter 4 is a good introduction to the determination of primary structure, although, since the book is designed for the beginner, I can see no reason for separating out modern methods from the more traditional methods. It would have been more instructive to have included these methods where appropriate. In Chapter 5, three-dimensional structure and folding is discussed. The 46 amino acid protein crambin is used in the first instance as an example and all elements of secondary structure are described. There is a small section on protein folding and the chapter concludes with some examples of how protein structure can be translated into a biological effect. A DNA binding protein, an antibody, and an enzyme are used as examples. I was glad that X-ray and NMR methods were mentioned but left as “black boxes” in this chapter but was rather unhappy that the role of the lone pair on the carbohydrate ring oxygen atoms was ignored in the mechanistic description of glycolysis. The final chapter deals with the use of computers in protein chemistry. Use of databases, modelling, sequence searching, evolution and structure prediction are all covered here.
In spite of some criticisms voiced above, I feel that this is an excellent introductory text to peptide and protein chemistry, an important interdisciplinary field which, with the growth of proteomics research, will become even more important in future.
ProfessorD. W. Young
Department of Chemistry, University of Sussex, UK
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