Prediction of the secondary structure of the carboxy-terminal third of rat thyroglobulin |
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| Authors: | S Formisano C Moscatelli R Zarrilli B Di Ieso R Acquaviva S Obici G Palumbo R Di Lauro |
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| Affiliation: | Faculty of Medicine, University of Oslo, Oslo, Norway;Faculty of Medicine, University of Oslo, Oslo, Norway;Faculty of Medicine, University of Oslo, Oslo, Norway;Faculty of Medicine, University of Oslo, Oslo, Norway;Faculty of Medicine, University of Oslo, Oslo, Norway;Faculty of Medicine, University of Oslo, Oslo, Norway |
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| Abstract: | A secondary structure prediction has been made using the available primary sequence data of the proposed carboxy-terminal of rat thyroglobulin. The model predicts 22% alfa-helix, 28% beta-structure and 17% beta turns. Out of the 8 possible carbohydrate acceptor-sites (Asn-x-Ser/Thr), 3 (residues 136, 368, 782) are associated with peptide sequences which favour the formation of beta-turn or loop-structures and are located in high hydrophilic regions. The entire sequence is predicted to be made up of two domains: one of them is highly structured, contains the hormonogenic sites, a cluster of tyrosines and at least one carbohydrate acceptor site. |
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