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CASE STUDY: Direct Characterization of Cysteine Binding in Signal Transduction Pathways by LC MS-MS

The characterization of disulfide-bridges and cysteine binding in proteins provided 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. Protea’s Bioanalytical Services team employs the most advanced mass spectrometry-based techniques and instrumentation to offer protein characterization studies which directly describe a protein’s three-dimensional structure as well as its structure-function relationships. In addition, this specificity of cysteine binding has been shown to play an important role in the regulation of protein-protein interactions and signal transduction pathways in biological systems.

This case study highlights the utility of high-resolution mass spectrometry analysis for the direct characterization of cysteine binding for protein-protein interactions. Data from a recent publication featuring work performed by Protea for one of our academic collaborators, conclusively demonstrated cysteine binding between Src SH2 domains and the cytoskeletal protein cortactin, presenting a new paradigm for SH2 domain functionality in domain-based signal transduction.


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