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Prediction for secondary structures of ten proteins from the 50S subunit of the escherichia coli ribosome

✍ Scribed by Dzionara, Michael ;Robinson, Stephen Michael Lewis ;Wittmann-Liebold, Brigitte

Publisher: Wiley (John Wiley & Sons)
Year: 1977
Tongue: English
Weight: 637 KB
Volume: 7
Category: Article
ISSN: 0091-7419
DOI: 10.1002/jss.400070204

No coin nor oath required. For personal study only.

✦ Synopsis

Abstract

Predictions of the secondary structures of the following 10 proteins from the large subunit of the E. coli ribosome were made using their known amino acid sequences: L6, L16, L19, L27, L28, L30, L31, L32, L33, and L34. The predictions were made according to 4 different methods and the results for each protein are presented as diagrams indicating the conformational states, helix, extended structure, turn, and random coil, of each residue. From these diagrams, regions of highly probable secondary structure for the proteins are calculated. Estimates are made of the maximum possible lengths of the proteins in order to correlate these with the results obtained from antibody binding sites in the 50S subunit as determined by electron microscopy.

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