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Modularity as an Organizing Principle in Protein Structure Unequal recombination drives the repetition of structural elements Titin x 300 Core of an average domain ~150 AA 20 different amino acids –> 20150 = 10195 different sequences Of these ~1038 are expected to have different fold (i.e. less than 20% sequence identity) Estimated number of naturally occurring folds ~1000 Fraction of theoretically possible “folds” used in nature ~ 1/1034 = 0.00000000000000000000000000000001% Super secondary Structure elements Unequal recombination drives the repetition of structural elements Titin x 300 TIM barrel muramidase Structures with alpha-hairpin motifs beta-hairpin Motifs beta-alpha-beta Motif QuickTime™ and a TIFF (Uncompressed) decompressor are needed to see this picture. Proteins with more than 30% AA identity almost always adopt the same fold. Stability -Gfolding Proteins as “Islands of Stability” in Sequence Space folded unfolded Sequence Bridges in between islands QuickTime™ and a TIFF (Uncompressed) decompressor are needed to see this picture. Cordes et al. Nat. Struct. Biol 2000 Dec;7(12):1129-32. QuickTime™ and a TIFF (Uncompressed) decompressor are needed to see this picture. QuickTime™ and a TIFF (Uncompressed) decompressor are needed to see this picture. QuickTime™ and a TIFF (Uncompressed) decompressor are needed to see this picture. Glykos, N.M., Cesareni, G. & Kokkinidis, M. (1999), Structure 7, 597-603 Paracelsus Challenge < 50% of AA changed B1 domain of protein G Janus
