Recognition of proximally phosphorylated tyrosine residues and continuous analysis of phosphatase activity using a stable europium complex.
作者： Sarah H. Hewitt , Roanna Liu , Stephen J. Butler
DOI: 10.1080/10610278.2017.1410548
关键词:
摘要: The recognition of proteins and their post-translational modifications using synthetic molecules is an active area research. A common modification the phosphorylation serine, threonine or tyrosine residues. proximal residues occurs in over 1000 human proteome, including disease-related proteins, so this motif particular interest. We have developed a luminescent europium(III) complex, [Eu.1] + , capable discrimination proximally phosphorylated residues, from analogous mono- non-phosphorylated more distantly-related phosphotyrosine serine was used to continuously monitor phosphatase catalysed dephosphorylation peptide containing
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