- Email: [email protected]
Sequencing of Proteins and Peptides
123
Sequencing of Proteins and Peptides b y G Allen. pp 327. Elsevier/North-Holland Biomedical Press, Amsterdam. 1981. D r 163 or 61 (paperback). ISBN 0-444-80254-1 and 0-444-80275-4 The test of any book is ultimately the usage it receives. Using this criterion as assayed over the last few months, the above text must rate fairly highly in its acceptability to protein sequencers - not the easiest of biochemical types to please! There are many books which deal with this topic and they all are deficient in some way. In this case, however, the errors/ omissions are the lowest yet for such a comprehensive cover. The text is fairly up-to-date, dealing as it does with some (but unfortunately not the most successful) methods employed in the study of very hydrophobic integral membrane proteins, a relatively new and different challenge for protein chemists. It is a compact volume providing easy access to the huge variety of (but not necessarily efficient!) techniques available for the determination of amino acid sequence. The information is presented in a sensible chronological order starting with methods employed in the purification and characterisation of proteins and progressing through chapters dealing in considerable detail with the generation, purification, detection, analysis and sequencing o f peptides. All the current strategies are mentioned and many of the incidental comments/tips are informative. Where detail is lacking, a suitable reference is nearly always quoted. In such texts, adequate referencing is critically essential and we have yet to find ourselves at a 'dead end'! For non-sequencers, some of the procedures could appear a little like biochemical witchcraft but the author's introduction of specific examples can prove not only instructive but reassuring, particularly since some of the newer methods are a little lacking in their theoretical bases. A full list of approaches is essential, for, depending on the protein under investigation, many procedures still belong to the 'suck it and see' brigade. The wide variation in protein structure is adequately catered for by the inclusion of chapters deahng with posttranslational amino acid modifications and their implications, microsequencing strategies and integral membrane proteins. It is also very helpful, and unusual, for equipment and reagent suppliers to be listed, for methods for reagent purification to be described and for safety matters to be discussed. These areas one suspects are likely to be subject to more and quicker changes than the remainder of the text. This is not a book for amateurs or marginally interested onlookers, of course, but on balance it is probably the best laboratory guide for protein sequencers currently available every sequencing home should have one; it's cheaper than QuadrolI Michael Brett
Sulfur in Proteins b y Y M Torchinsky (translated b y W Wittenberg). pp 294. Pergamon Press, Oxford. 1981 (original in Russian, 1977). $96 ISBN 0-08-023778-9 This monograph deals with the chemical properties and biological functions o f sulphur-containing groups present in proteins. The original edition appeared in Russian in 1977, but it is claimed that the English edition has been updated to include literature to 1979, as well as new figures and other material. Chapters 1-3 deals with the properties of -SH, -S-S-, and -S-CH3 groups in amino acids; Chapter 4 is on quantitative methods for sulphydryl and disulphide determination, and Chapter 5 is on differential reactivity of sulphydryl groups in proteins. This completes the first section of the book, the second section being on the role of sulphur-containing groups in enzymes and proteins.
BIOCHEMICAL
EDUCATION
10(3) 1982
After a chapter on methods of identifying essential -SH groups in enzymes, their role is considered with numerous examples. Chapter 8 deals with thiol cofactors (glutathione, lipoic acid, coenzyme A, etc), and incidentally has the structure of 4-phosphopantatheme wrong. Chapter 9 deals with the function of -S-S- bonds in proteins such as RNase, insulin, immunoglobulins, peptide hormones and keratins, while Chapter 10 deals briefly with the role of methionine in proteins. The final two chapters are on acid-labile sulphur in electron-carrier proteins (difficult to summarise in a few pages), and on chemical methods for introduction of sulphurcontaining groups into proteins. There are over 1800 references, but because the book is produced from typescript, the list occupies about 40 pages. The typescript is in fact reasonably easy to read and it is commendable that the formulae have been set to high standards. This would be a useful b o o k for undergraduates looking for essay material and also to graduate students and researchers about to go into the field of sulphur in proteins. People actually in the field would need more detail. C Jones
Protein-Protein I n t e r a c t i o n s Edited b y C Frieden and L W Nichol. pp 403. John Wiley & Sons, Chichester, UK. 1981. £33.45. ISBN 0-471-04979-4 This is a multi-author compilation that aims to discuss not only the experimental methods for the study of ProteinProtein Interactions but also the chemical bases and the biological consequences of these interactions. Nichol himself, and with D J Winzor, contributes the first and last chapters which deal largely with the theoretical aspects, namely definition patterns of protein interactions, and binding equations and control effects. The second chapter by Banasak, Birktoft and Barry is 'Protein-protein interactions and protein structures' and has a large appendix on the energetic aspects of protein-protein interactions. Chapter 3 by Winzor, deals with mass migration methods - gel chromatography, sedimentation velocity and electrophoresis, and chapter 4, by Cox and Dale, deals with the simulation o f transport experiments. Chapter 5, by Jeffrey, is on equilibrium methods: the basic equations are developed, the problem of the evaluation of the monomer concentrations is discussed, as is the analysis of interactions. Hammes, in Chapter 6, deals with fluorescence methods, and Frieden, in Chapter 7, considers how the picture changes if the proteins under study have enzymic activity. Finally, chapter 8, by Timasheff, is on the self-assembly of long, rod-like structures: a consideration o f the theoretical aspects is followed by a brief section on the methods that may be applied, with most of the examples from tubulin polymerization. The authors of the chapters are all well-known for their contributions in the various parts of this difficult field. The present volume is hardly an undergraduate text but would be o f interest to graduate students embarking on research topics in this general area. E J Wood
Carbon-13 NMR Spectral Problems by R B Bates and W A Beavers. pp 259. The Humana Press, Clifton, NJ, USA. 1981. ISBN 0-89603-010-5 or 0-89603-016-4 (paperback). A useful book for organic chemistry students designed to develop practical competence in the interpretations of Carbon-13 NMR Spectra. Contains 125 problems covering terpenes, amino acids and peptides, vitamins, natural and synthetic polymers, nucleic acid derivatives, hormones, drugs and organometallic compounds. Answers are given by reference to the literature sources of the spectra only.
Sequencing of Proteins and Peptides b y G Allen. pp 327. Elsevier/North-Holland Biomedical Press, Amsterdam. 1981. D r 163 or 61 (paperback). ISBN 0-444-80254-1 and 0-444-80275-4 The test of any book is ultimately the usage it receives. Using this criterion as assayed over the last few months, the above text must rate fairly highly in its acceptability to protein sequencers - not the easiest of biochemical types to please! There are many books which deal with this topic and they all are deficient in some way. In this case, however, the errors/ omissions are the lowest yet for such a comprehensive cover. The text is fairly up-to-date, dealing as it does with some (but unfortunately not the most successful) methods employed in the study of very hydrophobic integral membrane proteins, a relatively new and different challenge for protein chemists. It is a compact volume providing easy access to the huge variety of (but not necessarily efficient!) techniques available for the determination of amino acid sequence. The information is presented in a sensible chronological order starting with methods employed in the purification and characterisation of proteins and progressing through chapters dealing in considerable detail with the generation, purification, detection, analysis and sequencing o f peptides. All the current strategies are mentioned and many of the incidental comments/tips are informative. Where detail is lacking, a suitable reference is nearly always quoted. In such texts, adequate referencing is critically essential and we have yet to find ourselves at a 'dead end'! For non-sequencers, some of the procedures could appear a little like biochemical witchcraft but the author's introduction of specific examples can prove not only instructive but reassuring, particularly since some of the newer methods are a little lacking in their theoretical bases. A full list of approaches is essential, for, depending on the protein under investigation, many procedures still belong to the 'suck it and see' brigade. The wide variation in protein structure is adequately catered for by the inclusion of chapters deahng with posttranslational amino acid modifications and their implications, microsequencing strategies and integral membrane proteins. It is also very helpful, and unusual, for equipment and reagent suppliers to be listed, for methods for reagent purification to be described and for safety matters to be discussed. These areas one suspects are likely to be subject to more and quicker changes than the remainder of the text. This is not a book for amateurs or marginally interested onlookers, of course, but on balance it is probably the best laboratory guide for protein sequencers currently available every sequencing home should have one; it's cheaper than QuadrolI Michael Brett
Sulfur in Proteins b y Y M Torchinsky (translated b y W Wittenberg). pp 294. Pergamon Press, Oxford. 1981 (original in Russian, 1977). $96 ISBN 0-08-023778-9 This monograph deals with the chemical properties and biological functions o f sulphur-containing groups present in proteins. The original edition appeared in Russian in 1977, but it is claimed that the English edition has been updated to include literature to 1979, as well as new figures and other material. Chapters 1-3 deals with the properties of -SH, -S-S-, and -S-CH3 groups in amino acids; Chapter 4 is on quantitative methods for sulphydryl and disulphide determination, and Chapter 5 is on differential reactivity of sulphydryl groups in proteins. This completes the first section of the book, the second section being on the role of sulphur-containing groups in enzymes and proteins.
BIOCHEMICAL
EDUCATION
10(3) 1982
After a chapter on methods of identifying essential -SH groups in enzymes, their role is considered with numerous examples. Chapter 8 deals with thiol cofactors (glutathione, lipoic acid, coenzyme A, etc), and incidentally has the structure of 4-phosphopantatheme wrong. Chapter 9 deals with the function of -S-S- bonds in proteins such as RNase, insulin, immunoglobulins, peptide hormones and keratins, while Chapter 10 deals briefly with the role of methionine in proteins. The final two chapters are on acid-labile sulphur in electron-carrier proteins (difficult to summarise in a few pages), and on chemical methods for introduction of sulphurcontaining groups into proteins. There are over 1800 references, but because the book is produced from typescript, the list occupies about 40 pages. The typescript is in fact reasonably easy to read and it is commendable that the formulae have been set to high standards. This would be a useful b o o k for undergraduates looking for essay material and also to graduate students and researchers about to go into the field of sulphur in proteins. People actually in the field would need more detail. C Jones
Protein-Protein I n t e r a c t i o n s Edited b y C Frieden and L W Nichol. pp 403. John Wiley & Sons, Chichester, UK. 1981. £33.45. ISBN 0-471-04979-4 This is a multi-author compilation that aims to discuss not only the experimental methods for the study of ProteinProtein Interactions but also the chemical bases and the biological consequences of these interactions. Nichol himself, and with D J Winzor, contributes the first and last chapters which deal largely with the theoretical aspects, namely definition patterns of protein interactions, and binding equations and control effects. The second chapter by Banasak, Birktoft and Barry is 'Protein-protein interactions and protein structures' and has a large appendix on the energetic aspects of protein-protein interactions. Chapter 3 by Winzor, deals with mass migration methods - gel chromatography, sedimentation velocity and electrophoresis, and chapter 4, by Cox and Dale, deals with the simulation o f transport experiments. Chapter 5, by Jeffrey, is on equilibrium methods: the basic equations are developed, the problem of the evaluation of the monomer concentrations is discussed, as is the analysis of interactions. Hammes, in Chapter 6, deals with fluorescence methods, and Frieden, in Chapter 7, considers how the picture changes if the proteins under study have enzymic activity. Finally, chapter 8, by Timasheff, is on the self-assembly of long, rod-like structures: a consideration o f the theoretical aspects is followed by a brief section on the methods that may be applied, with most of the examples from tubulin polymerization. The authors of the chapters are all well-known for their contributions in the various parts of this difficult field. The present volume is hardly an undergraduate text but would be o f interest to graduate students embarking on research topics in this general area. E J Wood
Carbon-13 NMR Spectral Problems by R B Bates and W A Beavers. pp 259. The Humana Press, Clifton, NJ, USA. 1981. ISBN 0-89603-010-5 or 0-89603-016-4 (paperback). A useful book for organic chemistry students designed to develop practical competence in the interpretations of Carbon-13 NMR Spectra. Contains 125 problems covering terpenes, amino acids and peptides, vitamins, natural and synthetic polymers, nucleic acid derivatives, hormones, drugs and organometallic compounds. Answers are given by reference to the literature sources of the spectra only.