Peptide data on the disulfide bond analysis of baculovirus produced Pfs25 by LC-MSMS.

ABSTRACT: This article contains the peptide data obtained while performing disulfide bond mapping of the recombinant Plasmodium falciparum protein, Pfs25, produced from the baculovirus expression system. Pfs25 is a malaria transmission-blocking vaccine candidate, with a compact and complex structure including 22 cysteines. This supplementary data is related to the research "Disulfide bond mapping of Pfs25, a recombinant malaria transmission blocking vaccine candidate" (Lee et al., 2018) [1]. In brief, Pfs25 was digested with trypsin/Lys-C and derived peptides separated by High Performance Liquid Chromatography (HPLC) and analyzed by mass spectrometry (MS) by MS^E fragmentation. The theoretical peptides and their respective masses along with disulfide bond locations with linked pepti

SUBMITTER: Lee SM 

PROVIDER: S-EPMC5996233 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature