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Synthesis and characterization of histidine-phosphorylated peptides

✍ Scribed by Katalin F. Medzihradszky; Nancy J. Phillipps; Lionel Senderowicz; Ping Wang; Christoph W. Turck

Publisher
Cold Spring Harbor Laboratory Press
Year
1997
Tongue
English
Weight
683 KB
Volume
6
Category
Article
ISSN
0961-8368

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✦ Synopsis

Posttranslational phosphorylation of proteins is an important event in many cellular processes. Whereas phosphoesters of serine, threonine, and tyrosine have been studied extensively, only limited information is available for other amino acids modified by a phosphate group. The formation of phosphohistidine residues in proteins was discovered originally in prokaryotic organisms, but also has been found recently in eukaryotic cells. We describe methods for the synthesis and analysis of phosphohistidine-containing peptides, a prerequisite for the investigation of the role of this posttranslational modification in cellular processes.

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## Abstract Nano‐electrospray tandem mass spectrometry (nano‐ES‐MS/MS) was used to record collision‐induced dissociation (CID) spectra of a set of peptoid–peptide hybrids and the complete peptoid derived from the phosphopeptide Ac‐pTyr‐Glu‐Thr‐Leu‐NH~2~ (1). The presence of B and Y″‐type fragment i