Creative Biolabs has strong expertise in tyrosine sulfation sites prediction as well as protein tyrosine sulfation analysis. Scientists of Creative Biolabs have developed a robust and novel platform for sulfation site identification. We are confident in providing highly-effective services to meet special demands of our global customers.
Tyrosine sulfation is one of the universal post-translational modifications (PTMs), in which some sulfate groups are added to the tyrosine. Tyrosine sulfation often occurs in the transmembrane and secreted proteins. There has found that nearly 1% of all tyrosine residues of the total proteins in an organism can be sulfated.
Importance of tyrosine sulfation site prediction
Tyrosine sulfation plays an important role in the interactions between proteins and the modulations of the intracellular proteins. In addition, dysregulation or malfunction of tyrosine sulfation can result in serious diseases, such as atherosclerosis, lung diseases, and HIV infections. Therefore, it is essential to identify the protein tyrosine sulfation substrates and sites, which is also valuable in studying the molecular mechanism of tyrosine sulfation in biological processes and systems. Several experimental and predictive methods have been developed to identify the sites of tyrosine sulfation. However, there are many limitations on the identification the diverse sulfation sites.
In order to further understand the mechanism of tyrosine sulfation and enhance the quality of protein tyrosine sulfation sites prediction, Creative Biolabs provides a novel computational platform called IdentSulsite™, which can predict tyrosine sulfation sites from protein primary sequences. It incorporates protein secondary structure, physicochemical properties of amino acids and residue sequence order information.
Four main processes on IdentSulsite™ platform
Combined with our advanced methods, we can extract feature information protein primary sequences and construct several prediction models to study the influences of different sequences. These prediction models with multiple specialties have achieved very high accuracy in 10-fold cross-validation. These features can reflect the information of residues surrounding tyrosine sites. Finally, we also present the powerful web server, which is a successful predictor of predicting the tyrosine sulfation sites from primary protein sequences. A number of experimental results have shown that our prediction platform is more effective than the existing tyrosine sulfated prediction methods.
Fig.1 Analyses of three types of features around the tyrosine sulfation sites and the nonsulfated tyrosine sites (Huang et al. 2012).
Scientists of Creative Biolabs are confident in providing the cost-effective and high-quality tyrosine sulfation sites prediction services and using our platform to assist the discovery of important protein modifications. For more detailed information, please feel free to contact us or send us an inquiry.
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