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The following is a summary of visual aids (slides, artefacts and demonstrations) that may be found helpful in presenting the material in this book. Material for slides may be found in this book in the further reading at the ends of the chapters and in other readily available sources (indicated by references [1] to [5] and listed at the end of Appendix 2). Where material for slides needs to be found from more specialised publications and reports we have given appropriate references. Copyright permission should, of course, be obtained where applicable. 

Figure 15.17 The three-dimensional structure of an intact IgG. Hinge regions connecting the Fab arms with the Fc stem are relatively flexible, despite the presence of disulfide bonds in this region linking the heavy and light chains. Carbohydrate residues that bridge the two Ch2 domains are not shown. (Courtesy of A. McPherson and L. Harris, Nature 360 369-372, 1992, by copyright permission of Macmillan Magazines Limited.)...

A view down the fivefold symmetry axis of the icosahedtal structure (a) shows that the central capsomer is pentameric in shape and surrounded by five other capsomers as expected. The view down the pseudosixfold axis (h) shows, however, that the central capsomer is pentameric in shape and not hexameric as required for a T = 7 structure. (Adapted from 1. Rayment et al., Nature 295 110-115, 1982, hy copyright permission of Macmillan Magazines Limited.)... 

Figure 18.20 The two-dimensional NMR spectrum shown in Figure 18.17 was used to derive a number of distance constraints for different hydrogen atoms along the polypeptide chain of the C-terminal domain of a cellulase. The diagram shows 10 superimposed structures that all satisfy the distance constraints equally well. These structures are all quite similar since a large number of constraints were experimentally obtained. (Courtesy of P. Kraulis, Uppsala, from data published in P. Kraulis et ah. Biochemistry 28 7241-7257, 1989, by copyright permission of the American Chemical Society.)...

Figure 2 The bound structures of paromomycin and hygromycin B in helix 44 of the 30S subunit. Two nucleotides in helix 44, A1492 and A1493, are labeled, as are rings i-iv of paromomycin and rings I—IV of hygromycin B (from Brodersen et al. [4] with copyright permission).

Ribosomal Protein Synthesis Inhibitors. Figure 4 The binding site of pactamycin on the 30S subunit. The positions of mRNA, the RNA elements H28, H23b, H24a, and the C-terminus of protein S7 are depicted in the E-site of the native 30S structure (left) and in the 30S-pactamycin complex (right). In the complex with pactamycin, the position of mRNA is altered (from Brodersen etal. [4] with copyright permission). 

Fig. 7. Neurohumoral control of the metabolic changes during the acute phase of septic shock. AVP, vasopressin SNS, sympathetic nervous system TAG, triacylglycerol FFA, free faty acid. (Reproduced with permission from Clin. Endocrinol. K. N. Frayn, 24,577-599, 1986, by copyright permission of Blackwell Science Ltd., Oxford, UK.)...

Reproduced from Kistenmacher et al.2 with IUCr s copyright permission)... 

No part of this publication may be reproduced, stored in a retrieval system or transmitted in any form or by any means, electronic, mechanical, photocopying, recording or otherwise, without the prior written permission of the publisher, Elsevier Science B.V., Copyright Permissions Department, P.O. Box 521,... 

Figure 13.8. Solubility curves of chymotiypsinogen A in two different solvents. Adapted from J. H. Northrop, M. Kunitz, and R. M. Heiriot, Crystalline Enzymes, 2nd ed., Columbia University Press, New York, 1948. Originally published in J. Gen. Physiol. 24, 196 (1940) reproduced by copyright permission of the Rockefeller University Press.

MAFF/ADAS, 1986, pp. 150-151 with Crown Copyright Permission). 

The EC official method is described in the Official Journal of the European Communities (EC, 1992), and uses specialized glassware. We will base the method on that of MAEE/ADAS (1986, pp. 90-92), (with Crown Copyright permission), but replace the alcohol and diethyl ether (used for washing the residue) with acetone, which is safer and also used in the EC method. The AOAC method is described by Padmore (1990, pp. 80-82). The traditional method uses 0.313 M NaOH, free from carbonate, but the EC method uses 0.23 M KOH. The method is suitable for plant material or animal feeds, but the following pre-treatments may be necessary, especially for feedstuffs. 

This modification to the ADF method was designed to improve the relationship between the ADF and digestibility in ruminants. The sample drying temperature of 95°C, however, means it is unsuitable for assaying heat damage and unavailable protein (Van Soest, 1982). The method below is based on that given in MAFF/ADAS (1986, pp. 93-94), with Crown Copyright permission. See Chapter 4 for further discussion on fibre extraction procedures. 

Fig. 2. Recirculating, rack-type zebrafish system. A system made by Aquaneering, Inc., that provides multi-phase filtration, including a biological filter, and the ability to use tanks ot various sizes on the same system. The light-tight boxes shown on two rows ot the system here are an optional feature that allows for independent control of the light cycle tor each ot the enclosed rows. (Photograph and copyright permission kindly provided by Aquaneering, Inc.).

Fig. 1. Ribbon diagrams of Dictyostelium discoideum G-actin (Matsuura et al., 2000) and the Ascaris suum aMSP dimer (Bullock et al., 1996) at the same magnification. Actin consists of four subdomains that surround a nucleotide-binding cleft. The G-actin molecule is asymmetric, so that when it polymerizes, the filament it forms has a characteristic polarity and its two ends differ structurally. By contrast, MSP does not contain a nucleotide binding site and the polymerizing unit is a dimer in which the two MSP molecules are related by twofold rotational symmetry. Polymerization produces filaments composed of two helical subfilaments in which the dimers twofold axes are oriented perpendicular to the helix axis. Consequently, the MSP helices have no polarity and the subfilament ends are identical structurally (Bullock et al., 1998). Reproduced from The Journal of Cell Biology, 2000, vol. 149, pp. 7-12 by copyright permission of the Rockefeller University Press.

Fig. 3. Leading edge dynamics can be reconstituted in vitro using cell-free extracts of Ascaris sperm in which vesicles derived from the plasma membrane induce the assembly of MSP filament meshworks called fibers that push the vesicles forward as they elongate. The two images were taken 10 sec apart. Bar, 2.5 /im. Reproduced from The Journal of Cell Biology, 1999, vol. 146, pp. 1087-1095 by copyright permission of the Rockefeller University Press.

Fig. 6. Proposed push-pull model for nematode sperm locomotion. Assembly and bundling of MSP filaments into fiber complexes (dark band spanning the lamellipo-dium) pushes the membrane at the leading edge forward. At the same time a second force, associated with disassembly of the fiber complexes at the base of the lamellipo-dium, pulls the cell body forward. In this model, attachments where the cytoskeleton is linked to the membrane and the membrane anchored to the substratum establish traction and separate mechanically the forces produced at opposite ends of the fiber complexes. Thus, rather than canceling each other, these forces can be exerted independently against the substratum. Reproduced from The Journal of Cell Biology, 2000, vol. 149, pp. 7-12 by copyright permission of the Rockefeller University Press.

Fig. 5. Serial study of a woman with systemic lupus erythematosus showing correlation among levels of immune complexes measured by the Raji assay, complement levels, antibodies to native DNA, and clinical activity. (Reproduced with permission, A. N. Theofilopoulos, C. B. Wilson, and F. J. Dixon,. Clin. Invest. 57, 169-182, 1976, by copyright permission of the American Society for Clinical Investigation.)...

I express deep sense of gratitude to the various publishers for giving copyright permission to reproduce the following articles in the book ... 

Fig. 1. Areas of world with high average solar radiation levels (boxes). Copyright permission granted by Encyclopedia Britannica.

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