title: Finding the missing link: disulfide-containing proteins via a high-throughput proteomics approach.
abstract: Top-down proteomics have recently started to gain attention as a novel method to provide insight into the structure of proteins in their native state, specifically the number and location of disulfide bridges. However, previous techniques still relied on complex and time-consuming protein purification and reduction reactions to yield useful information. In this issue of Proteomics, Zhao et al. (high-throughput screening of disulfide-containing proteins in a complex mixture, Proteomics 2013, 13, 3256-3260) devise a clever and rapid method for high-throughput determination of disulfides in proteins via reduction by tris(2-carboxyethyl)phosphine. Their work provides the foundation necessary to undertake more complex experiments in biological samples.
authors.affiliation: Health Sciences Division, Department of Cell and Molecular Physiology, Loyola University Chicago, Maywood, IL, USA.
authors.forename: Ramzi J
authors.initials: RJ
authors.lastname: Khairallah
authors.forename: Sakthivel
authors.initials: S
authors.lastname: Sadayappan
mesh_terms: D004220:Disulfides / Q000032:analysis*; D057166:High-Throughput Screening Assays / Q000379:methods*; D011506:Proteins / Q000737:chemistry*
chemical_list: D004220:Disulfides; D011506:Proteins
keywords: Disulfide; Glutathionylation; Mass spectrometry; Post-translational modification; Redox modifications; Redox proteomics