Deglycosylation in Protein Mass Spectrometry
Protein mass spectrometry is an essential technique in biotechnology for analyzing protein composition, structure, and properties. In protein mass spectrometry, deglycosylation is commonly used to remove glycan moieties from proteins, allowing determination of their intact molecular weight. Mass spectrometry analysis following deglycosylation provides key insights, including the intact molecular weight of the protein, the glycosylation sites, and structural information.
Intact Molecular Weight of the Protein
Following deglycosylation, the protein’s molecular weight changes. By comparing the mass difference before and after deglycosylation, the mass of glycans originally attached to the protein can be determined.
Identification of Glycosylation Sites
The molecular weight shift caused by deglycosylation enables the localization of glycosylation sites, which is crucial for understanding protein modifications and their functional implications.
Structural Insights into the Protein
The attachment pattern and location of glycans influence the spatial conformation of a protein. Deglycosylation facilitates a deeper understanding of protein structure by revealing how glycosylation affects its folding and stability.
MtoZ Biolabs, an integrated chromatography and mass spectrometry (MS) services provider.
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