Secondary Structures of Proteins from the 30S Subunit of theEscherichia coliRibosome

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Abstract
The secondary structures of the proteins S4, S6, S8, S9, S12, S13, S15, S16, S18, S20 and S21 from the small subunit of the E. coli ribosome were predicted according to 4 different methods. From the resultant diagrams indicating regions of helix, turn, extended structure and random coil, average values for the respective secondary structures could be calculated for each protein. Using the known relative distances for residues in the helical, turn and sheet or allowed random conformations, estimates are made of the maximum possible lengths of the proteins to correlate these with results obtained from antibody binding studies to the 30S subunit as determined by EM. The influence of amino acid changes on the predicted secondary structures of proteins from a few selected mutants was studied. The altered residues tend to be structurally conservative or to induce only minimal local changes.