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Protein Science, Vol 6, Issue 7 1405-1411, Copyright © 1997 by Cold Spring Harbor Laboratory Press

ARTICLE

Synthesis and characterization of histidine-phosphorylated peptides

K. F. MEDZIHRADSZKY, N. J. PHILLIPPS, L. SENDEROWICZ, P. WANG and C. W. TURCK
Department of Pharmaceutical Chemistry, Mass Spectrometry Facility, University of California San Francisco, School of Pharmacy, Parnassus, U-6, San Francisco, California 94143-0446

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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