H-Thr-Glu-Pro-Glu-Tyr(PO₃H₂)-Gln-Pro-Gly-Glu-NH₂ contains a phosphorylated tyrosine that enables studies of kinase recognition and phospho-dependent signaling motifs. Its acidic residues support conformational exploration in extended peptide states. Researchers assess folding to understand charge-driven structural behavior. The molecule contributes to mapping phospho-regulated interaction sites.
1. Low bone turnover and low BMD in Down syndrome: effect of intermittent PTH treatment
2. Store-operated Ca2+ entry sustains the fertilization Ca2+ signal in pig eggs
4. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
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