Disulfide bond is a single covalent bond formed between the sulfur atoms of cysteines. The other sulfur-containing amino acid, methionine, cannot form disulfide bonds. Because it is a covalent bond, disulfide bond is often considered to be the primary structure. However, the function of disulfide bonds are far more than components of primary protein structure, they play a very important role in stabilizing the tertiary and quartenary structures, and are the prerequisite of proteins’ proper biological function.
Function of disulfide bonds
Given the ability of stabilizing overall structure of proteins, disulfide bridges are cross-linked in many commercialized proteins to increase their resistance to destructive effects of extreme environment used in industrial processes or protect protein-based therapeutics from rapid proteolytic degradation. Manufacturing of these products must take into account oxidative refolding—a formation of native disulfide bonds by specific pairs of cysteines located throughout a sequence of linear protein.
Creative Proteomics has established a highly sensitive HPLC-MS/MS platform that can analyze disulfide bonds in multiple samples and in both eukaryotic and prokaryotic organisms. In addition, we have optimized our protocol to enable more fast and sensitive site mapping service for disulfide bond analysis.
Applications of disulfide bond analysis service:
Creative Proteomics also provide the following bioinformatics services in Protein Post-translational Modification Analysis:
Functional annotation and enrichment analysis
Proteomic analysis of post-translational modifications
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