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Mass spectrometry (MS) is an analytical technique used to improve the study of these proteins on the proteome level. Glycosylation contributes to several concerted biological mechanisms essential to maintaining physiological function. The study of the glycosylation of proteins is important to understanding certain diseases, like cancer, because ...
Her focus has been on developing high-throughput technologies "to isolate and identify two of the most abundant protein modifications - phosphorylation and glycosylation." [ 1 ] Zhang applies proteomics technologies to determine protein modifications associated with cancer, which may improve early detection and monitoring of therapeutic care.
One of the purposes of this field of study is to determine which proteins are glycosylated and where in the amino acid sequence the glycosylation occurs. [4] Historically, mass spectrometry has been used to identify the structure of glycoproteins and characterize the carbohydrate chains attached. [4] [10]
A mass spectrometer used for high throughput protein analysis. Protein mass spectrometry refers to the application of mass spectrometry to the study of proteins.Mass spectrometry is an important method for the accurate mass determination and characterization of proteins, and a variety of methods and instrumentations have been developed for its many uses.
Glycosylation is a form of co-translational and post-translational modification. Glycans serve a variety of structural and functional roles in membrane and secreted proteins. [2] The majority of proteins synthesized in the rough endoplasmic reticulum undergo glycosylation.
MRM is a mass spectrometry-based technique that has recently been used for site-specific glycosylation profiling. Although MRM has been used extensively in metabolomics and proteomics, its high sensitivity and linear response over a wide dynamic range make it especially suited for glycan biomarker research and discovery.
The identification tag will vary depending on the type of analysis being done: biotin and click chemistry handles are suitable for enrichment of labeled proteins prior to mass spectrometry based identification, while fluorescent dyes are used when using a gel-based imaging method, such as SDS-PAGE, to validate interaction with a target. [7] [9]
Electron-capture dissociation (ECD) is a method of fragmenting gas-phase ions for structure elucidation of peptides and proteins in tandem mass spectrometry. It is one of the most widely used techniques for activation and dissociation of mass selected precursor ion in MS/MS.