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Alpha/Beta Folds

Index to Section 10

Alpha + Beta Folds

Alpha/Beta Doubly-Wound Folds



The doubly wound alpha/beta topology was described on the previous page. Some variations of the classic doubly wound fold are illustrated here. In the topology diagrams below, the parts of the chain linking the beta-strands are red, and are thick when they include an alpha-helix. In the RasMol scripts, non-alpha-helical linking regions are shown in pink. Some of the scripts highlight in blue where the fold begins.

flavodoxin, 1flv (127Kb) [Bbk|BNL|ExP|Waw|Hal] ... SCRIPT

subtilisin, 1sbt (172Kb) [Bbk|BNL|ExP|Waw|Hal] ... SCRIPT

arabinose-binding protein, domain 1, 5abp (217Kb) [Bbk|BNL|ExP|Waw|Hal] ... SCRIPT

glyceraldehyde phosphate dehydrogenase, 3gpd (443Kb) [Bbk|BNL|ExP|Waw|Hal] ... SCRIPT

dihydrofolate reductase, 3dfr (157Kb) [Bbk|BNL|ExP|Waw|Hal]

adenylate kinase, 3adk (135Kb) [Bbk|BNL|ExP|Waw|Hal]

rhodanese domain 1, 1rhd (202Kb) [Bbk|BNL|ExP|Waw|Hal]

glutathione reductase, 1gra (366Kb) [Bbk|BNL|ExP|Waw|Hal]

carboxypeptidase, 2ctb (Kb) [Bbk|BNL|ExP|Waw|Hal] This fold varies considerably from a classic doubly-wound variation in order to achieve the arrangement of sheet (mixed parallel and antiparallel in this case).

15Kb GIF


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Alpha/Beta Folds

Index to Section 10

Alpha + Beta Folds

Last updated 7th April '97