IVMR in detail

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IVMR in detail Protein NMR Techmques

edited by David 6. Reid, Hurrrarla Press, 1997. CJS$79. 50 hbk (x + 4 19 pafesj

ISBN 0 89603 309 0

It is now potsible to determine the three-dmlensional structures of

proteins of up to 20 kl)a routinely

with nuclear-magnetic-resonance

(NMR) techniques, provided that the protein can be obtained in

large-enough quantities and is

soluble and stable at room

temperature over a period of days.

Even though the methods are well

established, NMR is still a

complicated and labour-intensive

procedure. After obtaining a

number of multidimensional NMR

spectra, the NMR signals have to

be assigned to the nuclei that

produce them and structural

information has to be extracted.

The structure can then be

calculated using computer software.

Ptvteitz A’MR Techniques is a

collection of reviews covering a

wide range of topics concerned

with NMR on proteins. Six

chapters describe the path from

sample preparation to protein-

structure calculation. One chapter is

concerned with the production and

characterization of NMR samples

and another with the setting-up and

calibration of the NMR

spectrometer for the demanding

experiments on proteins. A third

chapter focuses on the variety of

heteronuclear experiments that are

currently available and suggests

strategies for their effective use to

obtain all the necessary mformation

for the assignment of NMR

spectra. Two chapters deal with the

computational side of obtaining a

structure: the first describes all the

methods and tricks necessary to

process the raw data mto NMR

spectra in such a way that a maximum of information is

combined with a minimum of

artefacts; the second explains the

various approaches to calculating the structure of the protein from

the available NMR data. Finally, a

case study is presented, giving an overview of the determination of

the structure of a small protein.

In addition, Prutein NMR

Techniques contains five more-or-

less separate chapters, which deal

with the nature of chemical shifts

and their (future) use in structure

calculations, the study of

protein-hgand interactions with

NMR, paramagnetic proteins,

Hitting the Target? Protein Targeting, Frontiers in Molecular Biology Series

edited by Hurtley M. Stella, O.rford Science P~rhlic~tions, 1996. UKL29.95 pbk

(xii + 214pages) ISBN 0 199 63561 7

This volume is a collection of

articles, written by experts in their

respective fields, reviewing most of

the major protein-targeting events

in eukaryotic cells. The first four

chapters deal with the delivery of

proteins to mitochondria, nuclei,

peroxisomes and the endoplasmic

reticulum (ER), the last three being

concerned with the sorting of

proteins within the endomembrane

system, focusing on ER-to-go@

and intragolgi traffic, the biogenesis

of secretory vesicles, and sorting

during endocytosis. In general, the

chapters provide a clear and

NMR studies on membrane-

associated peptides and proteins, and NMR on tnetal nuclei in

metalloproteins.

NMR on macromolecules has

become too wide a field to be

covered by a single book. Many

excellent books are available,

describing, for example, only the

practical or theoretical aspects.

Therefore, any new book should

have a clearly defined subject and

readership. This appears to be

lacking in J’rorein XMR Techniques.

The range of subjects is rather wide and, while some chapten are

concise introductions into a

particular subject, others are

elaborate and sometimes rather

technical reviews, more suitable as a

reference for specialists than as an

introduction. However, it should

be stressed that most chapters are,

in themselves, of high quality,

clearly explaining the important

points and with very up-to-date

references. Despite this, the book as

a whole is not a very good

introduction to protein NMR for

the biochemist who is considering

taking the plunge into structural determination using NMR. It

should instead be considered to be a collection of excellent

reviews that will form a useful

contribution to the bookshelf of

any NMR lab.

Marcellus Ubbink

Leiden Institute of Chemistry, Gorlaeus

Laboratories, PO Box 9502, 2300 RA

Leiden, The Netherlands. (Email: [email protected])

reasonably up-to-date account of an

important and fast-moving area.

Many of the articles are extensively

illustrated with line diagrams and tables, and otien provide a very

useful bibliography.

Perhaps inevitably in such a fast-

moving field, some articles are

already dated. New nomenclatures

for genes and mutants have been

adopted by the mitochondrial and

peroxisomal communities that

should make papers in this area much easier to follow in future. It

is especially disappomting that the

chapter on nuclear import did not

include the work on ‘importin’

from Gijrlich et al. The first paper

was published in 1991, and so

TIBTECH JANUARY 1998 (VOL 16)

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book ZLws

should have appeared in time for inclusion, if only as a note added in proof I found one or two silly mistakes that should have been eliminated at the proof stage, such as ‘chaperonins’ used when ‘chaperones’ was meant, and the specificity of the ERD2 receptor in K. lartic is surely DDEL not KKEL?

In the preface, the editor explains the decision to exclude prokaryotic systems and choloroplasts - to keep the book to a manageable size and because it was felt that ‘the general principles that are emerging [from the study of chloroplast protein targetingl are very similar to what has been learnt by looking at mitochondrial import’. Although I sympathize with the need to draw the line somewhere, restricting coverage to eukaryotic systems means that a great opportunity was lost to emphasize the evolutionary similarity between secretion of proteins from bacteria and the targeting of proteins to the ER that has become apparent in the past couple of years through the cloning

of the proteins of the Se&I complex from eukaryotic cells and the discovery of the bacterial signal recognition particle. In a similar fashion, I would argue that the targeting of proteins to chloroplasts, although sharing general principles with mitochondrial protein targeting, is fundamentally different from it. None of the receptor or channel components share any sequence similarity at all with previously identified mitochondrial proteins, although they may function analogously. implying convergent (rather than divergent) evolution in the fonnation of these organelles. Furthermore, GTP hydrolysis is implicated in chloroplast protein targeting and import as it is in the ER, but this is not the case m mitochondria. Chloroplasts are more complex than mitochondria, in that they possess an internal membrane network, the thylakoids, and (for reasons best known to themselves) thylakoid proteins require four different import pathways, two of

which share an obvious evolutionary origin with the prokaryotic ancestor of chloroplasts and one of which is clearly unique. The omission of bacteria and choloroplasts means that these underlying evolutionary similarities do not come through, despite the assertlon that ‘common principles will emerge’ through reading the different chapters of the book, which, as a consequence, is unnecessarily biased to mammalian systems.

In conclusion, this is a useful, if incomplete, collection of articles and, if not quite ‘frontier’ material any more, will be of use as an advanced undergraduate text and for research workers entering the field or wanting to keep abreast of developments in areas related to their own interests.

Alison Baker

Centre for Plant Biochemistry and Biotechnology, University of Leeds, Leeds,

UK LS2 9JT. (E-mall: [email protected])

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