Structural analysis of a highly acetylated protein using a curved-field reflectron mass spectrometer
UMass Chan AffiliationsDepartment of Biochemistry and Molecular Pharmacology
Amino Acid Sequence
Cell Cycle Proteins
Molecular Sequence Data
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
p300-CBP Transcription Factors
Amino acid sequencing
Matrix-assisted laser desorption/ionization-time of flight
Enzymes and Coenzymes
MetadataShow full item record
AbstractMatrix-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 cleavage 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.
SourceProteomics. 2005 Jun;5(9):2288-96. Link to article on publisher's site
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/50077
At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.
Related ResourcesLink to Article in PubMed