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Synthesis and characterization of histidine‐phosphorylated peptides
Author(s) -
Medzihradszky Katalin F.,
Phillipps Nancy J.,
Senderowicz Lionel,
Wang Ping,
Turck Christoph W.
Publication year - 1997
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560060704
Subject(s) - histidine , serine , phosphorylation , biochemistry , threonine , tyrosine , amino acid , chemistry , protein phosphorylation , posttranslational modification , biology , enzyme , protein kinase a
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.