Direct Characterization of Cysteine Binding in Signal Transduction Pathways by LC MS/MS

The characterization of disulfide-bridges and cysteine binding in proteins provides incredible insight to investigators focused on developing innovative biotherapeutic strategies (such as monoclonal antibodies). Using mass spectrometry to determine a protein therapeutic’s higher order structure and confirm its proper folding is quickly becoming an industry standard for describing the critical relationship between structure, function, and efficacy. This case study highlights the utility of high-resolution mass spectrometry analysis for the direct characterization of cysteine binding for protein-protein interactions.