Maximizing Selective Cleavages at Aspartic Acid and Proline Residues for the Identification of Intact Proteins.

ABSTRACT: A new approach for the identification of intact proteins has been developed that relies on the generation of relatively few abundant products from specific cleavage sites. This strategy is intended to complement standard approaches that seek to generate many fragments relatively non-selectively. Specifically, this strategy seeks to maximize selective cleavage at aspartic acid and proline residues via collisional activation of precursor ions formed via electrospray ionization (ESI) under denaturing conditions. A statistical analysis of the SWISS-PROT database was used to predict the number of arginine residues for a given intact protein mass and predict a m/z range where the protein carries a similar charge to the number of arginine residues thereby enhancing cleavage at aspartic acid resid

SUBMITTER: Foreman DJ 

PROVIDER: S-EPMC6207472 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature