book review: protein and peptide analysis by mass spectrometry. edited by j. r. chapman

1
BOOKS ~~ _____ ~~~ publication describing the example of the reaction. In addition it is possible to re- quest information about the catalytic cycle on which the reaction is based and the relevant reaction parameters (sub- strate, substitution pattern, nucleophile, leaving groups, etc.). The catalytic cycle and the list of reaction parameters can al- so be found in identical form in the Hand- book of Palladium-Catalyzed Organic Re- actions. c) Probably the most effective way of using the data bank is by means of the various search facilities that are provided. These allow one to specify keywords relat- ing to the solvent, catalyst, reaction con- ditions, ligands, yield, and authors. By carrying out a search with two or more simukaneous criteria one can limit the number of matching reactions that it pro- duces and thus arrive more quickly at the required data. One can also perform a search in which these criteria are com- bined with a chosen reaction scheme de- scribed by using the ISIS/Draw facility. In fact, however, it is often advantageous to use such a reaction scheme by itself, either by searching directly for the reaction that the scheme depicts, or by carrying out a search to list all those reactions in which the structures of the educt and product are present as subunits. In another type of sit- uation one’s interest might lie not in a par- ticular reaction but in reactions that in- volve a given substrate. In that case the program allows olie to specify the sub- strate structure together with a reaction arrow and obtain a list of all reactions in which that structure is present, either in its own right or as a subunit. In a similar way one can also carry out a search to find a synthesis giving a particu- lar product. Thus, the Database of Palladium Chem- istry provides a toolkit that affords the user rapid access to important informa- tion of all kinds. Furthermore, the data bank is to be kept up-to-date by con- tinually adding new reactions, typically at a rate of 500-700 each year. That prospect will be of great interest to every- one concerned with organopalladium chemistry. Franz Zumpe Organisch-Chemisches Institut der Universitat Heidelberg (Germany) Protein and Peptide Analyis by Mass Spectrometry- Edited by J. R. Chap- man. (Series: Methods in Molecular Biology, Vol. 61.) Humana Press, Totowa, 1996. 350 pp., hardcover $69.50.-ISBN 0-896-03345-7 J. R. Chapman has already edited sev- eral successful books on mass spectrome- try. The present book of 21 chapters is concerned with applications of modern mass spectrometric methods to the analy- sis of proteins and peptides. In the first, introductory chapter P. Roepstorff gives a short summary of the past and present development of mass spectrometry. Here also the work of the late Michael Barber, ‘father’ of FAB ion- ization, to whom the book is dedicated, is honored. Then follows an introduction to mass spectrometry by Chapman, in which soft ionization methods, mass analyzers, and modern techniques such as MS/MS are explained. The choice of the topics of the subse- quent chapters is well balanced and covers many current analytical problems in protein chemistry. However, special prob- lems of synthetic peptide chemistry, such as the characterization of synthetic pep- tides or analytical problems of combina- torial chemistry, are not discussed. Some of the topics dealt with in detail are the determination of the primary structure of proteins by tandem mass spectrometry, by low- and high-energy CID, PSD or ladder sequencing, mass spectrometric finger- printing for the identification and charac- terization of proteins, determination of post-translational modifications (deter- mination of the disulfide bridges), and the analysis of gIycopeptides and protein con- jugates. Also quantitative aspects are dis- cussed in one chapter (quantitative analy- sis of neuropeptides) . Further chapters deal with the secondary structural analy- sis of proteins, the determination of non- covalent (supramolecular) interactions of proteins, the computer-assisted analysis of mass spectra, and the identification of proteins by means of protein databases. Since the chapters have been written by different authors (all of whom are recog- nized experts in the field of biochemical mass spectrometry), one might expect some overlapping and repetition. Fortu- nately, however, this is not the case. The individual chapters are on different and well-demarcated topics, and repetitions are rare (one of the few exceptions: a table containing the masses of the amino acid residues appears both in Chapter 12 and in Appendix 111). In accordance with their increasing im- portance for protein analysis, the two modern soft ionization techniques of elec- trospray ionization (ESI) and matrix- assisted laser desorption ionization (MALDI) are treated most thoroughly. Nevertheless, the classical methods such as SIMS und FAB have not been forgot- ten. As usual for books of the series Meth- ods in Molecular Biology, each chapter is organized in sections entitled ‘Introduc- tion’, ‘Materials’, ‘Methods’, and ‘Notes’. These sections contain much advice and many practical tips, so that the scientist with the required analytical equipment at his disposal can put the particular method into practice right away in his own labora- tory. At the end of each chapter is a bibli- ography, which also, commendably, in- cludes very recent literature (up to the year 1996). In addition the appendix con- tains over 180 further references, most of them from 1995. The text is well illustrated by numerous figures and tables and contains only a few typing errors (e.g., p. 322, ‘Vat’ instead of ‘Val’; p.327, ‘Tryp’ instead of ‘Trp’). The subject index could be more detailed. Some terms, such as ‘FTMS’ or ‘ion trap’, which occur in the text, are not listed here. The book provides the protein chemist with comprehensive information about the capabilities of modern mass spec- trometry for biopolymer analysis. Be- cause it is also helpful for practical appli- cations in the laboratory (for example in explaining which detergents interfere with the analysis of proteins by ESI-MS), it can be recommended unreservedly for all scientists working in the field of protein chemistry. Before one picks up this book, however, one should take seriously the warning that Chapman gives in the pref- ace: ‘the use of mass spectrometry might be habit-forming’! Jorg W Metzger Institut fur Siedlungswasserbau der Universitat Stuttgart (Germany) 2253 Angen,. Chem. Int. Ed. Engl. 1997,36, No. 20 0 WILEY-VCH Verlag GmbH. D-694.51 Weinheim, 1997 0570-083319713620-22.53 $17.50+..50;0

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Page 1: Book Review: Protein and Peptide Analysis by Mass Spectrometry. Edited by J. R. Chapman

BOOKS ~~ _____ ~~~

publication describing the example of the reaction. In addition it is possible to re- quest information about the catalytic cycle on which the reaction is based and the relevant reaction parameters (sub- strate, substitution pattern, nucleophile, leaving groups, etc.). The catalytic cycle and the list of reaction parameters can al- so be found in identical form in the Hand- book of Palladium-Catalyzed Organic Re- actions.

c) Probably the most effective way of using the data bank is by means of the various search facilities that are provided. These allow one to specify keywords relat- ing to the solvent, catalyst, reaction con- ditions, ligands, yield, and authors. By carrying out a search with two or more simukaneous criteria one can limit the number of matching reactions that it pro- duces and thus arrive more quickly at the required data. One can also perform a search in which these criteria are com- bined with a chosen reaction scheme de- scribed by using the ISIS/Draw facility. In fact, however, it is often advantageous to use such a reaction scheme by itself, either by searching directly for the reaction that the scheme depicts, or by carrying out a search to list all those reactions in which the structures of the educt and product are present as subunits. In another type of sit- uation one’s interest might lie not in a par- ticular reaction but in reactions that in- volve a given substrate. In that case the program allows olie to specify the sub- strate structure together with a reaction arrow and obtain a list of all reactions in which that structure is present, either in its own right or as a subunit. In a similar way one can also carry out a search to find a synthesis giving a particu- lar product.

Thus, the Database of Palladium Chem- istry provides a toolkit that affords the user rapid access to important informa- tion of all kinds. Furthermore, the data bank is to be kept up-to-date by con- tinually adding new reactions, typically at a rate of 500-700 each year. That prospect will be of great interest to every- one concerned with organopalladium chemistry.

Franz Zumpe Organisch-Chemisches Institut

der Universitat Heidelberg (Germany)

Protein and Peptide Analyis by Mass Spectrometry- Edited by J. R. Chap- man. (Series: Methods in Molecular Biology, Vol. 61.) Humana Press, Totowa, 1996. 350 pp., hardcover $69.50.-ISBN 0-896-03345-7

J. R. Chapman has already edited sev- eral successful books on mass spectrome- try. The present book of 21 chapters is concerned with applications of modern mass spectrometric methods to the analy- sis of proteins and peptides.

In the first, introductory chapter P. Roepstorff gives a short summary of the past and present development of mass spectrometry. Here also the work of the late Michael Barber, ‘father’ of FAB ion- ization, to whom the book is dedicated, is honored. Then follows an introduction to mass spectrometry by Chapman, in which soft ionization methods, mass analyzers, and modern techniques such as MS/MS are explained.

The choice of the topics of the subse- quent chapters is well balanced and covers many current analytical problems in protein chemistry. However, special prob- lems of synthetic peptide chemistry, such as the characterization of synthetic pep- tides or analytical problems of combina- torial chemistry, are not discussed. Some of the topics dealt with in detail are the determination of the primary structure of proteins by tandem mass spectrometry, by low- and high-energy CID, PSD or ladder sequencing, mass spectrometric finger- printing for the identification and charac- terization of proteins, determination of post-translational modifications (deter- mination of the disulfide bridges), and the analysis of gIycopeptides and protein con- jugates. Also quantitative aspects are dis- cussed in one chapter (quantitative analy- sis of neuropeptides) . Further chapters deal with the secondary structural analy- sis of proteins, the determination of non- covalent (supramolecular) interactions of proteins, the computer-assisted analysis of mass spectra, and the identification of proteins by means of protein databases.

Since the chapters have been written by different authors (all of whom are recog- nized experts in the field of biochemical mass spectrometry), one might expect some overlapping and repetition. Fortu-

nately, however, this is not the case. The individual chapters are on different and well-demarcated topics, and repetitions are rare (one of the few exceptions: a table containing the masses of the amino acid residues appears both in Chapter 12 and in Appendix 111).

In accordance with their increasing im- portance for protein analysis, the two modern soft ionization techniques of elec- trospray ionization (ESI) and matrix- assisted laser desorption ionization (MALDI) are treated most thoroughly. Nevertheless, the classical methods such as SIMS und FAB have not been forgot- ten.

As usual for books of the series Meth- ods in Molecular Biology, each chapter is organized in sections entitled ‘Introduc- tion’, ‘Materials’, ‘Methods’, and ‘Notes’. These sections contain much advice and many practical tips, so that the scientist with the required analytical equipment at his disposal can put the particular method into practice right away in his own labora- tory. At the end of each chapter is a bibli- ography, which also, commendably, in- cludes very recent literature (up to the year 1996). In addition the appendix con- tains over 180 further references, most of them from 1995.

The text is well illustrated by numerous figures and tables and contains only a few typing errors (e.g., p. 322, ‘Vat’ instead of ‘Val’; p.327, ‘Tryp’ instead of ‘Trp’). The subject index could be more detailed. Some terms, such as ‘FTMS’ or ‘ion trap’, which occur in the text, are not listed here.

The book provides the protein chemist with comprehensive information about the capabilities of modern mass spec- trometry for biopolymer analysis. Be- cause it is also helpful for practical appli- cations in the laboratory (for example in explaining which detergents interfere with the analysis of proteins by ESI-MS), it can be recommended unreservedly for all scientists working in the field of protein chemistry. Before one picks up this book, however, one should take seriously the warning that Chapman gives in the pref- ace: ‘the use of mass spectrometry might be habit-forming’!

Jorg W Metzger Institut fur Siedlungswasserbau

der Universitat Stuttgart (Germany)

2253 Angen,. Chem. Int. Ed. Engl. 1997,36, No. 20 0 WILEY-VCH Verlag GmbH. D-694.51 Weinheim, 1997 0570-083319713620-22.53 $17.50+..50;0