Top-down study of β2-microglobulin deamidation.

ABSTRACT: Although differentiation of the isomeric Asn deamidation products (Asp and isoAsp) at the peptide level by electron capture dissociation (ECD) has been well-established, isoAsp identification at the intact protein level remains a challenging task. Here, a comprehensive top-down deamidation study is presented using the protein beta2-microglobulin (β(2)M) as the model system. Of the three deamidation sites identified in the aged β(2)M, isoAsp formation was detected at only one site by the top-down ECD analysis. The absence of diagnostic ions likely resulted from an increased number of competing fragmentation channels and a decreased likelihood of product ion separation in ECD of proteins. To overcome this difficulty, an MS(3) approach was applied where a protein ion was first fragmented by c

SUBMITTER: Li X 

PROVIDER: S-EPMC4170183 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature