Structural analysis of a highly acetylated protein using a curved-field reflectron mass spectrometer

Dongxia Wang, Paul Thompson, Philip A. Cole, Robert J. Cotter

Research output: Contribution to journalArticle

Abstract

Matrix-assisted laser desorption/ionization mass spectrometry and tandem mass spectrometry (MS/MS) were used to determine the multiple acetylation sites in the histone acetyltransferase (HAT): p300-HAT. Partial deavage of the peptides containing acetylated lysine residues by trypsin provided a set of nested sequences that enabled us to determine that multiple acetylation occurs on the same molecule. At the same time, cleavages resulting in a terminal unacetylated lysine suggested that not all of these sites are fully modified. Using MS and MS/MS, we were able to characterize both the unmodified and acetylated tryptic peptides covering more than 82% of the protein.

Original languageEnglish (US)
Pages (from-to)2288-2296
Number of pages9
JournalProteomics
Volume5
Issue number9
DOIs
StatePublished - Jun 1 2005

Keywords

  • Acetylation
  • Amino acid sequencing
  • Mass spectrometry
  • Matrix-assisted laser desorption/ionization-time of flight

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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