Prediction of the secondary structure of the carboxy-terminal third of rat thyroglobulin.
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.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002942:Circular Dichroism / Q000379:methods; D010446:Peptide Fragments; D011487:Protein Conformation; D051381:Rats; D013954:Thyroglobulin
D000596:Amino Acids; D010446:Peptide Fragments; D013954:Thyroglobulin