Glycoinformatics-assisted Mucin-type Glycosylation Site Prediction Service

Glycoinformatics-assisted Mucin-type Glycosylation Site Prediction Service

Unlocking the Potential of Glycoinformatics for Precise Glycosylation Predictions

With extensive experience in providing Glycoinformatics-assisted Analysis/Prediction Services, CD BioGlyco offers a comprehensive range of professional services including Glycoinformatics-based Structure Modeling Services and Structural and Functional Prediction Services. The details of our glycoinformatics-assisted mucin-type glycosylation site prediction service are as follows.

Machine learning models and bioinformatics analysis

Our experts first obtain mammalian protein sequence data and glycosylation site information from UniProt, and then build models to predict glycosylation sites based on this information. After obtaining protein sequence data and glycosylation site information, we analyze and organize these data, and use bioinformatics tools to perform sequence comparison, structure prediction, and other operations to identify potential glycosylation sites. Then, the machine learning algorithms or deep learning models are applied to build models for predicting glycosylation sites and evaluate the accuracy and reliability of the models through validation experiments. Our glycosylation site models use a variety of features, including amino acid sequences, secondary structures, relative accessibility of residues, physicochemical properties of amino acids, and features of amino acid sequences, to improve the accuracy of predictions.

Analysis of amino acid frequency near glycosylation sites

We perform detailed calculations and analysis of the frequency of amino acid presence around the glycosylation sites to more accurately estimate the probability of amino acid presence at each position relative to the glycosylation site. Through this, we help you gain insight into the distribution of amino acids at different positions in the protein structure, which provide an important reference for further studies of protein function and structure.

Process of glycoinformatics-assisted mucin-type glycosylation site prediction. (CD BioGlyco)

Publication

Technology: Computational prediction

Journal: International journal of molecular sciences

IF: 4.9

Published: 2010

Results: The researchers used support vector machines (SVMs) to predict glycosylation sites of mucins and found that glycosylation sites are usually aggregated in the sequence while other sites are dispersed in the sequence. Therefore, they developed two types of SVMs to predict aggregated and dispersed sites, respectively. They found that amino acid composition is effective for predicting aggregated glycosylation sites, while site-specific algorithms are effective for predicting dispersed glycosylation sites. The highest prediction accuracy for aggregated glycosylation sites was 74%, while the highest prediction accuracy for dispersed glycosylation sites was 79%. Independent component analysis revealed that the position-specific presence of amino acid sequences around glycosylation sites was an independent component. The researchers also found that the glycosylation sites of mucins were more likely to map to disordered regions of extracellular proteins.

Fig.1 Repositioning glycosylation sites to distinguish between the structural domains and intrinsically disordered regions of human glycoproteins.Fig.1 Repositioning of glycosylation sites to the differentiation between structural domains and ID regions of human glycoproteins. (Nishikawa, et al., 2010)

Applications

  • Glycosylation sites of mucins are closely associated with the onset and progression of several diseases. Techniques to predict these sites are used to help identify potential biomarkers for early disease prediction.
  • Techniques for predicting glycosylation sites are used to design targeted drugs and reduce drug side effects.
  • When engineering mucins to improve their properties or functions, techniques for predicting glycosylation sites are used to guide the gene editing or protein synthesis process, ensuring correct and efficient glycosylation.

Advantage

  • We combine our knowledge of bioinformatics and glycobiology to quickly and accurately predict mucin-type glycosylation sites, helping you get the information you need quickly.
  • Our experts provide reliable prediction results based on extensive experimental data and bioinformatics algorithms.
  • Our technology visualizes the predicted results, giving you a more intuitive view of the distribution of glycosylation sites, which aids in research and analysis.

Frequently Asked Questions

  • What is the rationale for predicting glycosylation sites?
    • Glycosylation is an important form of protein post-modification, which plays a key role in the occurrence and development of diseases. Predicting glycosylation sites can help researchers gain insight into the functions and regulatory mechanisms of disease-related proteins. Moreover, many drug targets are proteins, and the presence of glycosylation sites may affect the binding properties of drugs to proteins. Predicting glycosylation sites can provide important information for drug design and guide the rational design of drug structures.
  • What does mucin-based glycosylation mean?
    • In living organisms, protein molecules are usually combined with sugar molecules to form glycosylated proteins. Mucin-type glycosylation is a specific form of glycosylation in which sugar molecules bind to proteins to form specific glycosylation sites. This form of glycosylation plays an important role in biological processes such as cell signaling, cell surface interactions, and immune responses.

At CD BioGlyco, our experts utilize advanced bioinformatics tools and machine-learning algorithms to provide accurate and reliable predictions for mucin-type glycosylation sites. Trust us to enhance your research and development with our state-of-the-art prediction service. For further details, please don't hesitate to contact us.

Reference

  1. Nishikawa, I.; et al. Computational prediction of O-linked glycosylation sites that preferentially map on intrinsically disordered regions of extracellular proteins. International journal of molecular sciences. 2010, 3;11(12): 4991-5008.
For research use only. Not intended for any diagnostic use.
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