Collision induced dissociation products of disulfide-bonded peptides: ions result from the cleavage of more than one bond.

ABSTRACT: Disulfide bonds are a post-translational modification (PTM) that can be scrambled or shuffled to non-native bonds during recombinant expression, sample handling, or sample purification. Currently, mapping of disulfide bonds is not easy because of various sample requirements and data analysis difficulties. One step towards facilitating this difficult work is developing a better understanding of how disulfide-bonded peptides fragment during collision induced dissociation (CID). Most automated analysis algorithms function based on the assumption that the preponderance of product ions observed during the dissociation of disulfide-bonded peptides result from the cleavage of just one peptide bond, and in this report we tested that assumption by extensively analyzing the product ions generated wh

SUBMITTER: Clark DF 

PROVIDER: S-EPMC3543116 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature