Glycopeptide Identification
Glycopeptide Identification - Related Videos
10:11
Glycopeptide Capture for Cell Surface Proteomics
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Cited by 8 •
2014
Cell surface proteins are biologically important and widely glycosylated. We introduce here a glycopeptide-capture approach to solubilize, enrich, and deglycosylate these proteins for facile LC-MS based proteomic analyses.
14:02
Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry
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Cited by 30 •
2017
This paper describes a methodology to prepare cardiovascular tissue samples for MS analysis that allows for (1) the analysis of ECM protein composition, (2) the identification of glycosylation sites, and (3) the compositional characterization of glycan forms. This methodology can be applied, with minor modifications, to the study of the ECM in other tissues.
08:37
The Application of Open Searching-based Approaches for the Identification of Acinetobacter baumannii O-linked Glycopeptides
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Cited by 5 •
2021
Open searching enables the identification of glycopeptides decorated with previously unknown glycan compositions. Within this article, a streamlined approach for undertaking open searching and subsequent glycan-focused glycopeptide searches are presented for bacterial samples using Acinetobacter baumannii as a model.
14:12
Rodent Identification II
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2015
Source: Kay Stewart, RVT, RLATG, CMAR; Valerie A. Schroeder, RVT, RLATG. University of Notre Dame, IN Animal records must be accurately maintained to ensure that data collection is correct. Records range from maintaining information on cage cards to having a detailed database with all of the relevant information on each animal. The primary component of recordkeeping is the individual identification of research animals. There are a variety of methods suitable for identifying mice and rats. This...
11:09
Rodent Identification I
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2015
Source: Kay Stewart, RVT, RLATG, CMAR; Valerie A. Schroeder, RVT, RLATG. University of Notre Dame, IN A fundamental requirement of biomedical research is the proper identification of research animals. It is essential that the right animal is utilized for procedures and data collection. Laboratory mice and rats can be identified with the following permanent methods: ear tags, ear punch codes, microchip implantation, tail tattoos for adult mice, and toe tattoos for neonates. Temporary methods of...
FAQs
Accurate identification benefits from combining measured mass with fragmentation patterns. The mass provides evidence about the peptide and its attached carbohydrate, while tandem fragmentation supplies structural clues that help separate peptide sequence information from glycan composition and localize the attachment site. Using both readouts therefore strengthens assignment rather than relying on mass alone.
Attachment-site assignment depends on fragmentation evidence that retains information about where the carbohydrate is connected to the peptide. This is distinct from determining the peptide sequence or overall glycan composition. Resolving all three features gives a more informative molecular description for studying glycoprotein structure and regulation.
Mapping N-linked and O-linked glycosylation allows investigators to report which broad attachment categories occur within the analyzed peptides. That distinction supports structured comparisons of glycoprotein profiles, especially when samples differ by biological condition. It also helps connect observed carbohydrate patterns with questions about protein function and post-translational regulation.
Reliable assignments connect measured molecular features with biological interpretation. By establishing which peptide regions carry carbohydrate structures, the analysis can support investigations of protein structure, cell signaling, and post-translational regulation. This makes identification valuable not only for cataloging glycosylation, but also for explaining how altered glycoprotein states may relate to biological function.
A typical workflow begins by digesting proteins into peptides. The resulting mixture is then separated by liquid chromatography, which organizes compounds before measurement. Tandem mass spectrometry subsequently records peptide masses and fragmentation patterns. Interpreting these data together supports assignment of peptide sequence, glycan composition, and attachment site.
Researchers can compare glycoprotein profiles across biological conditions after identifying the relevant glycopeptides and their carbohydrate features. Differences in detected patterns provide a molecular basis for examining disease-related changes or other condition-associated shifts. The value lies in linking profile variation to altered glycosylation and potential changes in protein regulation.
It is particularly useful for characterizing biomarkers, therapeutic proteins, and disease-related changes. In these applications, identifying the peptide context together with carbohydrate composition and attachment site gives a molecular basis for comparing glycoprotein profiles. The findings can inform studies of protein structure, cell signaling, and post-translational regulation.