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prediction of n glycosylation sites in human proteins Empty prediction of n glycosylation sites in human proteins

Sat Nov 13, 2021 9:45 pm
Glycosylation, the process of attaching glycans to proteins or other organic molecules, is one of the most common post-translational modifications (PTMs). Glycans are highly branched carbohydrate structures, consisting of monosaccharide sugars, such as fucose, galactose, manose, sialic acid, and N-acetylglucosamine. Due to the complexity and diversity of composition and structure of glycans, and the site of glycan attachment, glycosylation may affect product stability, immunogenicity, serum clearance, pharmacokinetics, and anti-inflammatory activity. Therefore, glycosylation is a Critical Quality Attribute (CQA) that must be presented. Glycosylation analysis is critical step to ensure safety and potency of biopharmaceutical products during the process of drug discovery. prediction of n glycosylation sites in human proteins https://www.creative-proteomics.com/pronalyse/glycosylation-sites-and-oligosaccharides-analysis-service.html
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prediction of n glycosylation sites in human proteins Empty Re: prediction of n glycosylation sites in human proteins

Sat Nov 13, 2021 9:45 pm
Phosphorylation is a common post-translational modification (PTM) of proteins in eukaryotes, which functions in various cell activities, including glycolysis, protein-protein interaction, protein degradation, enzyme inhibition, homeostasis, and so forth. Protein phosphorylation is a reversible process of attachment of a phosphoryl group to proteins catalyzed by enzymes, principally on serine, threonine or tyrosine residues. Approximately 30% of proteins subject to phosphorylation in eukaryotic cells are tightly associated with protein activity by changing conformation of phosphorylated proteins. phosphorylation https://www.creative-proteomics.com/pronalyse/phosphorylation-protein-analysis-service.html
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prediction of n glycosylation sites in human proteins Empty Re: prediction of n glycosylation sites in human proteins

Sat Nov 13, 2021 9:45 pm
Therapeutic proteins products have been proven effective against various diseases. Complex post-translational modifications (PTMs) are required by most therapeutic proteins. Common PTMs include glycosylation, oxidation, deamidation, proteolysis, and so forth. These PTMS not only affect efficient secretion, drug efficacy and stability of therapeutic proteins, but also may influence safety, immunogenicity, serum clearance, pharmacokinetics, etc. deamidation https://www.creative-proteomics.com/pronalyse/deamidation-and-oxidation-analysis-service.html
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prediction of n glycosylation sites in human proteins Empty Re: prediction of n glycosylation sites in human proteins

Sat Nov 13, 2021 9:45 pm
The disulfide bond plays an important role in maintaining the spatial three-dimensional structure of peptides and proteins and the biological activity determined thereby, and is also related to the stability and renaturation of proteins. Analysis of disulfide bonds and free sulfhydryl groups on proteins helps to analyze the high-level structure of proteins to reveal the biological functions of proteins. Disulfide bond analysis can analyze the structural characteristics of protein to improve its degradation stability and prolong its efficacy. The analysis of disulfide bonds in proteins is an important biochemical technology for biotherapeutic drug development projects. Related technical methods can be used to determine the location and content of disulfide bonds of biopharmaceutical proteins or other biological agents, thereby determining the structure and relative molecular content of proteins, and also measuring free thiol groups. disulfide bridge https://www.creative-proteomics.com/pronalyse/disulfide-bridges-free-sulfhydryl-groups-analysis-service.html
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