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Book Review Protein Folding. By C. C. Ghlis and J. Yon

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VB calculations-except the most sophisticated ones-03
should possess the cyclic structure too.
Ozone participates in smog formation. This is the reason
why ozonation in the gas phase was developed mainly by
kineticists and ecologists. The embarrassing assumption
that ozone reacts with hydrocarbons in the gas phase in a
fundamentally different way than in solution, is becoming
extinct. The introductory 1,3-dipolar cycloaddition and the
subsequent 1,3-dipolar cycloreversion appear to be the
same in gas and liquid phase. It is only the recombination
of carbonyl oxide and carbonyl compound forming the
ozonide which is replaced in the gas phase by unimolecular conversions of the carbonyl oxide and secondary reactions.
Grousing about a monograph meeting such high standards would be bad style. The quality of presentation deserves recognition. Statements about temperature, solvent
and yields on the reaction arrows of the excellent formula
blocks would be valuable for the reader. The “diradical
structures” in the language of quantum chemists are sometimes falsely associated with reactivity by organic chemists.
The notion of the carbonyl oxide occurring as a diradical
in the gas phase and as a zwitterion in solution (p. 31)
should not be taken verbally.
Whoever has to do with ozonation will find enlightening
information in this standard work of reference written by
one of the foremost leaders in the field.
Rolf Huisgen [NB 616 IE]
Institut fur Organische Chemie
der Universitiit Munchen (FRG)
Protein Folding. By C. C. Ghelis and J. Yon. Academic
Press, New York 1982. xiii, 562 pp., bound, $ 74.50.
The present state of protein structure research is marked
by the completed crystal structure analyses of more than
one hundred proteins, the elucidation of the mechanism of
transcription and translation, as well as the possibilities for
the sequencing of proteins and (recently) also the nucleic
acids coding them. The result of all this is knowledge concerning the topology and detailed three-dimensional structure of globular protein molecules down to the atomic
level and the insight derived therefrom into the catalytic
mechanism of enzymes and into their evolutionary relationships.
Basically the functional state of proteins formed spontaneously both in vivo and in vitro represents the (kinetically
accessible) state of minimum free energy. Both this structure itself and the process of its formation are described as
“folding”. It is the last stage in the “translation” of the genetic information stored in the nucleic acid into a covalent
amino acid sequence and constitutes the last, largely unexplained, portion of the whole process of protein biosynthesis. Apart from the inborn curiosity of biochemists there
are two reasons why interest is concentrated on this problem: Firstly, it is of theoretical importance, because, if the
protein folding “code” were known, it would be possible,
on the basis of the structure-function relationship, to use
the nucleic acid sequences of otherwise uncharacterized
proteins (enzymes) to predict their structures and their
functions. Secondly, the “code” could be used to design
molecules for the optimization of desired catalytic functions.
[*] Cf. Angew. Chem. 91 (1979) 523; Angew. Chem. Int. Ed. Engl. 18 (1979)
Angew. Chem. l n t . Ed. Engl. 23 (1984) No. 4
Both aims can only be envisaged because the three-dimensional structure of proteins is determined solely by the
amino acid sequence of their polypeptide chains. This postulate made by Crick 25 years ago is based on the observation that protein molecules spontaneously revert to their
native conformations after disturbance of their structure
(denaturation) and are able to recover their biologically active state of association.
This present volume is devoted to the complex of questions outlined. It provides-apart from a volume of extended symposium contributions of the same name (Elsevier-North Holland, 1980)-the first comprehensive summary, and with its ca. 1500 literature references represents
a veritable treasure trove for newcomers in the field.
The authors have attempted to describe the whole
breadth and historical depth of the field, whereby they understand folding to have both systematic-descriptive aspects and energetic and kinetic ones. This leads to one of
the weaknesses of the book, namely its length (and thus its
price) together with a certain lack of criticality; the old and
the new are presented side by side, with no attempt to sift
and classify.
The book begins with a section on the intracellular environment and the significance of folding (30 pp.). Then follow almost 200 pages dealing with observations on the
problem of protein folding from the viewpoint of the characterization of globular proteins. This is followed by 275
pages concerned with experimental methods; the book
concludes with a 22-page summarizing commentary.
The above mentioned makeup and subdivision of the
book cited and the relative sizes of its parts give some idea
of the encyclopaedic proportions of the work. It is basically a detailed survey and not a more profound discussion
of chosen examples. This has the consequence for the interested reader that every time “classical” portions of the
subject are surveyed, the reader can obtain more detailed
information first hand (from the presentations of J. Richardson, Anfinsen and Scheraga, Baldwin, Creighton, Tanford for example). The qualitative nature of the presentation is particularly regrettable for those parts of the field
that become more and more accessible to a solid physicochemical treatment, e.g. intermolecular interactions (somewhat remarkably generally called intramolecular interactions), the structure of water, the thermodynamics and kinetics of unfolding and folding. Here it may also be a case
of what the authors themselves call “progressing on shifting sand” with reference to rapidly evolving topics such as
peptide ptocessing, topogenic (not topogenetic) sequences
and structural flexibility. The quality production of the
book and the necessary time span before its appearance
demand their price, particularly with respect to topicality.
In general the extraordinary amount of material and the
documentation of even the older literature are of assistance to those who wish an effortless introduction to parts
of the field. As previously stated a critical sifting of the
material and tautening with respect to questions that still
remain open would spare the reader some outdated matter.
That the reading is not always simple, lies in the problem
that “non-natives” who write in English frequently use an
unorthodox idiom, that can sometimes only be completely
understood after back translation. This remark is directed
at the publishers rather than at the authors. This is not the
case, however, with the subject index which is not really
adequate for a book of this encyclopaedic nature.
It would be out of place here to criticize individual
points ; however, the occasional aesthetic or teleological
arguments, the not always concise definitions, and the
fuzzy distinction in some places between the thermodynamic and the kinetic viewpoint are mentioned as being
symptomatic. Critical thinking is necessary on the part of
the reader in order to avoid falling into error.
The book can be of good service as a reference work,
both with regard to the various aspects of the subject and
for particular topics. It is to be hoped that it will arouse
biochemists and biophysicists to intensify research in one
of the most interesting areas of physical biochemistry today.
Ruiner Jaenicke [NB 619 IE]
Institut fur Biophysik und Physikalische Biochemie
der Universitat Regensburg (FRG)
Springer Series in Synergetics. Vol. 13: Handbook of Stochastic Methods for Physics, Chemistry, and the Natural
Sciences. By C. W. Gordimer. Springer-Verlag, Berlin
1983. xix, 442 pp., bound, ISBN 3-540-11357-6; Vol. 16:
Physics of Bioenergetic Processes. By L. A . Blumenfeld.
Volume editor: H . Huken. Springer-Verlag, Berlin 1983.
x, 132 pp., bound, DM 70.00.-ISBN 3-540-11417-3;
Vol. 20: Advanced Synergetics. Instability Hierarchies of
Self-organizing Systems and Devices. By H . Haken.
Springer-Verlag, Berlin 1983. xv, 356 pp., bound, DM
98.00.- ISBN 3-540-12 162-5
Polymere Werkstoffe. Vol. 11: Technologie 1. Edited by H.
Batzer. Georg Thieme Verlag, Stuttgart 1983, xiv, 434
pp., bound, DM 320.00 (subscription price DM
256.00).-ISBN 3-13-648201-8
Advances in Polymer Science. Vol. 52/53: Crazing in Polymers. Edited by H . H. Kausch. Springer-Verlag, Berlin
1983. ix, 347 pp., bound, DM 138.00.--1SBN 3-540-12571-x
Organisch-chemische Nomenklatur. Einfiihrung in die
Grundlagen mit Regeln und Beispielen. 2nd edition. By P.
Fresenius. Wissenschaftliche Verlagsgesellschaft, Stuttgart 1983. 280 pp., Paperback, DM 44.00.-ISBN 38047-0722-x
Polymer Science and Technology. Vol. 20: Polymer Alloys
111. Blends, Blocks, Grafts, and Interpenetrating Networks. Edited by D. Klempner and K . C. Frisch. Plenum
Press, New York 1983. ix, 302 pp., bound, $ 45.00.ISBN 0-306-41138-5
Technische Thermodynamik. By G. Meyer and E. Schiffner.
Verlag Chemie, Weinheim 1983. 375 pp., bound, DM
38.00. -ISBN 3-527-26034-X
Bioelektrochemische Membranelektroden. By J. G.
Schindler and M . M . Schindler. Walter de Gruyter, Berlin 1983. xii, 341 pp., bound, DM 180.00.-ISBN 3-11008790-1
Progress in Pesticide Biochemistry and Toxicology. Vol. 3.
Edited by D. H. Hutson and T. R . Roberts. Wiley Interscience, Chichester 1983. x, 449 pp., bound, .€ 54.50.ISBN 0-471-90053-2
Lecture Notes in Biomathematics. Vol. 51: Oscillations in
Mathematical Biology. Proceedings of a Conference
held at Adelphi University, April 19, 1982. Series editor:
S . Levin. Volume editor: J. P.E. Hodgson. Springer-Verlag, Berlin 1983. vi, 196 pp., Paperback, DM 32.50.ISBN 3-540-12670-8
The following corrections should be made to the
communication entitled: “Reactions of Diphenyl(trimethylsily1)phosphane with Alkyl(pentacarbony1)manganese;
(C0)4MhCr(OSiMe3)PPhz,and a New Driving Force for
CO Insertion” by John A. Gladysz et al., Angew. Chem.
Int. Ed. Engl. 23 (1984) 245:
The title should read: “Reactions of Diphenyl(trimethylsily1)phosphane with Alkyl(pentacarbony1)manganese;, Synthesis
(CO),MnCR(OSiMe3) Phz, and a New Driving Force for
CO Insertion”. The heading to column 2 in Table 1 should
read v(C = 0).
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Angew. Chem. Int. Ed. Engl. 23 (1984) No. 4
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