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Book Review Modern Methods in Protein- and Nucleic Acid Research. Edited by H. Tschesche

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Biochemistry, edited by A. J. Hoff (Elsevier), can be recommended.
Pulsed ESR methods are now at the beginning of a development that could follow a course analogous to the enormous qualitative improvement of NMR techniques that has
occurred in recent years. However, it remains to be seen
whether microwave pulses will “exorcize the evil from
ESR”-as
has happened in the case of NMR-thereby
opening a new “Golden Age” for ESR spectroscopy. Everyone who wishes to get to grips with these new and fascinating
techniques, or who even foresees possible applications in his
or her own research, is strongly recommended to read this
book. Regrettably, however, the very high price-which has
now become the rule rather than the exception for books of
this sort--will limit the potential readership.
Wolfgang Lubitz
Max-Volmer-Institut fur Biophysikalische
und Physikalische Chemie
der Technischen Universitat Berlin (FRG)
One Dimensional and Two Dimensional NMR Spectra by
Modern Pulse Techniques. Edited by K . Nukunishi. University Science Books, Mill Valley (USA), 1990. XII, 234 pp.,
paperback $29.95. - ISBN 0-935702-63-6
Yet another book on NMR methods has been published;
in this the aim is to convey a knowledge of NMR by means
of a catalogue of 92 experiments, rather than by a systematic
form of presentation. In accordance with the book‘s title, the
examples are arranged in two groups consisting of 31 onedimensional (1 D) and 61 two-dimensional (2D) experiments. Each experiment is described in about half a page of
text with a few literature references (in which the name Bodenhausen has been wrongly spelled in nearly every case),
together with a diagram showing the pulse sequence and the
structural formula of the compound. The spectrum is reproduced on the opposite page, edited in a form which corresponds to the structural formula, so that the assignments are
directly apparent. A set of parameter values is also shown
alongside the spectrum in most cases, although unfortunately these are often too small to be read clearly and are insufficient to enable one to do further work on the problem;
moreover, the accompanying text seldom includes experimental details.
The selection of experiments covers nearly all the standard
types of problems nowadays encountered in organic chemistry. Thus the 1 D part includes examples of techniques such
as NOE difference measurements, SPT, DEPT, selective decoupling, and suppression of water signals, while in the 2 D
part one finds, in addition to the expected variants of COSY
and NOESY, examples of HOHAHA, ROESY, and 2DINADEQUATE experiments.
There are a few key molecules, such as p-ionone or strychnine, that are used again and again as examples in the book,
thus enabling the reader to progress comfortably from simple types of spectra to more complicated types as applied to
the same molecule; this is undoubtedly one of the book’s
main strengths. On the other hand the examples chosen are
sometimes unnecessarily complicated, as in the cases of
brevetoxin (No. 56), cyanoviridin (No. 84), or dictyotalide
(No. Sl), which tend to obscure the merits of the techniques
under discussion rather than to clarify them. Nevertheless,
the book as a whole offers a wealth of stimulating ideas
taken from all the main research themes of organic chemistry, thus conveying to the reader some of the pleasure
Angew. Chem. Inf. Ed. Engl. 31 (1992) No. 2
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evoked by the power of modern NMR spectroscopy. The
spectra that are reproduced, which are certainly the main
substance of the book, are of better than average quality.
However, there are a few criticisms that must be mentioned.
For example: the convention of having the f , axis as the
horizontal one is not applied consistently; for inversely
recorded spectra (such as some of the examples of HMBC
and HMQC experiments), the fiprojection appears sometimes at the left-hand and sometimes at the right-hand border of the spectrum; too often some of the peaks of the
projection are allowed to protrude into the 2 D spectrum,
which to me appears rather inelegant. Here it becomes evident that the book is not a unified whole but a collection of
contributions from a number of spectroscopists using different spectrometers with different software.
There is a 40-page appendix entitled “Principles of FTNMR’, in which an attempt is made to explain the theory
behind the experiments that are included. Everyone is likely
to appreciate that a meaningful summary of the theory of
modern 1 D and 2 D multipulse NMR spectroscopy is not
possible within such a limited space, and consequently the
reader is unlikely to derive anything useful from this account.
In summary it can be said that this book offers, at a reasonable price, a stimulating survey of the NMR methods
nowadays used in organic chemistry. It can certainly be recommended for libraries and textbook collections, and for
serious organic chemists who wish to learn what their NMR
section should be capable of; it is less suitable for NMR
specialists, who need a more detailed knowledge of the subject than can be conveyed within the space of this book.
Stefun Berger
Fachbereich Chemie
der Universitat Marburg (FRG)
Modern Methods in Protein- and Nucleic Acid Research.
Edited by H . Tschesche. de Gruyter, Berlin, 1990. ix,
446 pp., hardcover DM 330.00.-ISBN 3-1 1-012275-8
This book can be regarded as a continuation of the series
“Modern Methods in Protein Chemistry”, previous volumes
ofwhich appeared in 1983, 1985, and 1988. The latest developments in analytical and preparative methods are here described in 20 review articles by well-known authors belonging mostly to German research groups. This volume is the
first to cover molecular biological methods. After a brief
introduction to the techniques, the methods are described in
turn using examples from each author’s own field of research, sometimes including an experimental section giving
practical details. Each article provides an up-to-date list of
references, including review articles and monographs. The
book is convenient to use and sturdily bound. However, the
authors’ typescripts have been directly reproduced, and the
resulting lack of uniformity in type style and line spacing is
rather distracting.
The first three articles are devoted to nucleic acids chemistry and molecular biology. H. Tschesche et al. describe the
use of digoxigenin-I 1-dUTP as a realistic alternative to radioactive labeling. w. Kramer and H.-J. Fritz discuss the
advantages and disadvantages of the various methods for
preparing mutants using oligonucleotide techniques. B. S.
Reckmann then describes new analytical procedures in DNA
diagnostics. H. Wagner and J. Heinrich kindle interest in free
flow electrophoresis, an elegant preparative electrophoretic
method for purifying peptides, proteins, and whole cells. Other innovations in the purification and isolation of proteins
Verlagsgesellschaj? mbH, W-6940 Weinheim, 1992
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245
are the use of new types of polymers that give improved
yields in ion-exchange chromatography (C. Jansen and W.
Miiller), and the use of immobilized nickel for affinity
chromatography applied to poly-His fusion proteins (E.
Hochuli). Problems of chain folding are addressed by R.
Rudolph using in-vitro redox reactions, and by P. Flecker
using activation chromatography; in the examples described
here both methods give highly active proteins. Advances in
C-terminal sequencing offer a method for the identification
of biomolecules, which is here critically compared with Nterminal sequencing (B. Wittmann-Liebold et al.). The introduction of cyclodextrin phases for the enantioselective analysis of amino-acids by gas chromatography can greatly
improve the separation achieved (W. A. Konig). New opportunities and capabilities in the use of mass spectrometry to
investigate biomolecules are described by E. Bayer. Soft ionspray mass spectrometry allows characterization of proteins
up to 120000 Dalton and sequencing of segments at picomolar concentrations. The technique also has impressive capabilities when combined on-line with capillary zone electrophoresis or HPLC. Next W. Voelter et al. describe what
can be achieved by immunological characterization. D. M.
Doran gives an excellent review and comparison of current
methods for predicting epitopes in proteins. Three articles
deal with modifications of nucleic acids and proteins. In the
first, R. I. Zhadanov reports on ESR studies of spin-labeled
Ca-ATPase. H. Fasold et al. describe interactions of proteins
with modified nucleotides. D. Brandenburg et al. give a thorough account of the use of photoafinity-labeling in combination with radioactive or biotin labeling for isolating and
characterizing receptors and for studying their interactions;
this comprehensive chapter includes practical advice, information on typical reagents and their areas of application,
and a list of common abbreviations. The last group of articles are concerned with methods for studying the structures
of proteins. “How do you get large protein crystals?” is the
title of the chapter by G. Wiegand, in which the crucial
factors in the various crystallization techniques are discussed
from a practical standpoint, illustrated by useful figures. J.
Reed gives a good review of circular dichroism measurements, their areas of application, the types of information
yielded, and the methods used to interpret the data. S. Suhai
describes the theoretically orientated approach of molecular
dynamics stimulation; unfortunately some of the diagrams
in this chapter are illegible. H. Riiterjans et al. complete the
treatment of protein structural studies by describing the application of 2D-NMR spectroscopy to ribonuclease-T, .
It is certainly not possible to describe the whole of protein
and nucleic acids research in 446 pages, but the editor has
neither attempted nor claimed to do that. Instead the book
is intended to give an insight into the latest developments. In
this it has succeeded outstandingly well. The choice of topics
represents the most significant trends in protein chemistry,
the main emphasis throughout being on the techniques. The
subject matter is logically arranged, and corresponds to the
many stages that are needed to express, isolate, and characterize a protein. As it is not possible for a single research
group to be completely knowledgeable in all these areas and
equipped to carry out the experimental work needed, progress can only be achieved through the interdisciplinary collaboration of many specialists. This book helps to overcome
trepidation about making the necessary contacts and to remove obstacles of technical language. Thus, for example, the
molecular biologist is introduced to expressions such as
NOESY and COSY, and the physical chemist learns to understand the problems of PCR methods. The book is of value
to everyone who wishes to look out beyond the limited confines of his or her own research. Furthermore, it should help
the reader to apply new methods without repeating familiar
mistakes.
Annette Beck- Sickinger
Laboratorium fur Biochemie
der Eidgenossischen Technischen Hochschule
Zurich (Switzerland)
Registered names, rrademorks, etc. used in (his journal. even when nor marked as such. are not to be considered unprorected by law.
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Editor: Perer C6litz
Associate editors: R. H. Schmidt-Radde, K . J Schneidcr, A. Stimron. Editorial assistant: E. Schweikarl
Publishers: VCH Verlagsgesellschaft mbH. (Managing Directors: Hans Dirk Mhfer. Dr. Karlheinz Kdp/er), Pappelallee 3, W-6940 Weinbeim, Federal Republic of Germany.
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