Statistical analysis of the glycol-protein landscape surrounding protein glycosylation sites aims to uncover information and patterns related to protein glycosylation. CD BioGlyco provides professional statistical analysis of glycoprotein landscapes around glycosylation sites leveraging our extensive experience in Glycosylation Site Statistical Analysis. The services we provide include but are not limited to the following:
We analyze the frequency of loop regions with varying surface areas, including α-helix, β-folding, and structureless regions, by calculating the accessible surface area of the protein surface. The purpose of this analysis is to gain insight into the structural basis of N-glycoprotein processing and maturation. For instance, examining the secondary structure in loop regions with different surface areas allows us to determine whether there is a higher occurrence of unstructured loop regions in immature glycosylation datasets. Thus, the loop region that is more likely to interact with the glycosyl moiety is identified.
We offer the amino acid frequency analysis service for you. The purpose of amino acid frequency analysis is to understand the frequency of occurrence of different amino acids in the glycoprotein structure around the N-glycosylation site. By analyzing the frequency of amino acids, the roles and effects of different amino acids in the N-glycosylation process and the maturation process can be revealed.
In addition, by categorizing amino acid residues into four groups (negatively charged, positively charged, hydrophobic, and hydrophilic), we determine which group of residues is relatively more common in immature glycoproteins for you.
We also analyze the structural characteristics of amino acid side chains, assisting in the examination of the frequency of occurrence of short and long-side chain amino acids surrounding mature and immature glycoproteins. This aids in uncovering their regulatory role in protein surface interaction with sugar groups.
Technology: Zwitterionic hydrophilic interaction liquid chromatography (ZIC-HILIC)
Journal: Frontiers in Chemistry
IF: 3.8
Published: 2021
Results: In this publication, the authors used a complete O-glycopeptide analysis strategy to analyze the O-glycosylation sites of the SARS-CoV-2 recombinant S protein and the O-glycosylation landscape in its vicinity. The authors used ZIC-HILIC for complete glycopeptide enrichment and PNGase F to remove non-glycopeptide and N-glycopeptide interference. Finally, the authors analyzed the intact O-glycopeptides using a high-resolution mass spectrometer and characterized and manually validated the mass spectra using Byonic software. Therefore, it can be concluded that the O-glycosylation landscape obtained by the authors was based on the analysis of intact glycopeptides near the glycosylation site.
Fig.1 Revealing the full scope of O-glycosylation on SARS-CoV-2 spike proteins through comprehensive profiling. (Zhang, et al., 2021)
With extensive experimental experience, CD BioGlyco provides tailored protocols to meet your specific requirements for statistical analysis of glycoprotein landscapes around glycosylation sites. Please feel free to contact us to discuss your specific needs.
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We envision a future where the intricate world of carbohydrate is no longer shrouded in mystery, but rather illuminated by the power of cutting-edge computational tools.