Disulfide bond is a type of post-translational modifications in proteins formed between the sulfur atoms of two cysteine residues during the biosynthesis of the proteins in the cell. Disulfide bonds are important in protein folding, they play a significant role in both protein structure and function. Therefore, the analysis of disulfide bond in proteins is of great significance to reveal the higher structure and biological functions of proteins. In addition, incorrect disulfide bond formation or exchange can cause antibody aggregation, so understanding the disulfide bonding is critical for protein characterization in the biopharmaceutical production process.
Figure 1. disulfide bonds in mature proteins
Creative Proteomics provides services to map the disulfide bond sites of unknown proteins and verify the disulfide bonds and folding structure of protein samples. Basic steps include peptide extraction, peptide separation and data analysis.
A variety of biological samples are available for testing, such as cell, animal tissue, blood, serum and so on.
|Blood (EDTA added)||1ml|
|Microbes||Dry weighed: 200mg|
|If you want to know specific sample requirements, please feel free to contact us.|
We are specialized in quantitative multiplexed proteomics and metabolomics applications through the establishment of state-of-the-art mass spectrometry platforms, and we have optimized sample processing methods and a series of advanced analytical methods that provide a strong guarantee for the success of the research. As every project has different requirements, please contact our specialists to discuss your specific needs. We are looking forward to cooperating with you.
1. Bošnjak I, Bojović V, Šegvić-Bubić T, et al. Occurrence of protein disulfide bonds in different domains of life: a comparison of proteins from the Protein Data Bank[J]. Protein engineering, design & selection, 2014, 27(3): 65-72.