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

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 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.

journal_name

Proteomics

journal_title

Proteomics

authors

Wang D,Thompson P,Cole PA,Cotter RJ

doi

10.1002/pmic.200401167

subject

Has Abstract

pub_date

2005-06-01 00:00:00

pages

2288-96

issue

9

eissn

1615-9853

issn

1615-9861

journal_volume

5

pub_type

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