Richardson, Jane

The Kinemage Supplement, produced by Jane Richardson at Duke University, is available from the publisher as a complement to this book for readers with access to a personal computer. The system is easy to use and provides interactive three-dimensional viewing of many of the structures discussed in various chapters. 

Figure 2.10 Examples of schematic diagrams of the type pioneered by Jane Richardson. Diagram (a) illustrates the structure of myoglobin in the same orientation as the computer-drawn diagrams of Figures 2.9b-d. Diagram (b), which is adapted from J. Richardson, illustrates the structure of the enzyme triosephosphate isomerase, determined to 2.5 A resolution in the laboratory of David Phillips, Oxford University. Such diagrams can easily be obtained from databases of protein structures, such as PDB, SCOP or CATH, available on the World Wide Web.

W.H. Freeman, 1988, after a drawing provided by Jane Richardson.)... 

FIGURE 6.7 The three-dimensional structures of two proteins that contain substantial amounts of rx-helix in their structures. The helices are represented by the regularly coiled sections of the ribbon drawings. Myohemery-thrin is the oxygen-carrying protein in certain invertebrates, including Sipunculids, a phylum of marine worm. (Jane Richardson)... 

FIGURE 6.23 The three-dimeiisioiial structure of bovine ribonuclease A, showing the o -hehces as ribbons. (Jane Richardson)... 

FIGURE 6.34 Sheet structures formed from andparallel arrangements of /3-strands, (a) Streptomyces suh i x Xu inhibitor, (b) glutathione reductase domain 3, and (c) the second domain of glyceraldehyde-3-phosphate dehydrogenase represent minimal andparallel /S-sheet domain structures. In each of these cases, an andparallel /S-sheet is largely exposed to solvent on one face and covered by helices and random coils on the other face. (Jane Richardson)... 

FIGURE 6.43 The polypeptide backbone of the prealbnmin dimer. The monomers associate in a manner that continnes the /3-sheets. A tetramer is formed by isologons interactions between the side chains extending outward from sheet D A G H HGAD in both dimers, which pack together nearly at right angles to one another. (Jane Richardson)... 

The association of secondary structures to give super-secondary structures, which frequently constitute compactly folded domains in globular proteins, is completed by the a-a motifs in which two a-helices are packed in an anti-parallel fashion, with a short connecting loop (Figure 4.8c). Examples of these three structural domains, often referred to as folds, are illustrated in Figures 4.9—4.11. The schematic representation of the main chains of proteins, introduced by Jane Richardson, is used with the polypeptide backbone... 

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