59. Disulfide Mapping Verification using SIEVE
Poster: Tue 2:00-3:00PM
Michael Athanas
Vast Scientific
View Long Abstract
Disulfide cross-linkages formed by the oxidation of the thiol groups of cysteines, play an important role in the folding and stability of many proteins. We studied two plasma derived coagulant proteins that are commercially available products from CSL Limited containing complex disulfide maps. Reduced+alkylated and non-reduced samples are processed with accurate mass LC-MS and analysized with SIEVE v1.3. Candidate ions are searched against a database containing all predicted peptides along with expected PTMs and all combinations of paired cysteine containing peptides. Measurements of relative peak abundance (presence / absence) can then be used to validate disulfide cross linkage across cysteines.