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Results: 4

1.
Fig. 4.

Fig. 4. From: Mapping Yeast N-Glycosites with Isotopically Recoded Glycans.

Relative frequencies of residues surrounding yeast N-glycosites. Sequences of the 133 unique glycosylation sites detected by directed LC-MS/MS are aligned on the modified Asn residue. Relative heights of the surrounding amino acids are adjusted based on the frequencies of their occurrence.

Mark A. Breidenbach, et al. Mol Cell Proteomics. 2012 June;11(6):M111.015339.
2.
Fig. 3.

Fig. 3. From: Mapping Yeast N-Glycosites with Isotopically Recoded Glycans.

Ontological analysis of high confidence N-glycoproteins. N-Glycoproteins were categorized according to the manually curated ontological annotations including cellular component (a), molecular function (b), and biological process (c) maintained by the Saccharomyces Genome Database (31).

Mark A. Breidenbach, et al. Mol Cell Proteomics. 2012 June;11(6):M111.015339.
3.
Fig. 2.

Fig. 2. From: Mapping Yeast N-Glycosites with Isotopically Recoded Glycans.

The perturbing effect of a GlcNAc isomix on a peptide isotopic envelope. a, simulated isotopic envelopes (z = 2) for the GlcNAc isomix (red trace), an unlabeled peptide from the glycoprotein Ygp1 (NSSSALNITELY, blue trace), and the same peptide labeled with the GlcNAc isomix (violet trace). The isotopically recoded peptide has a visually distinctive distribution of peak intensities. b, in experimental LC-MS data, the isotopic envelope of the precursor ion corresponding to the NSSSALnITELY glycopeptide is shown (the modified Asn residue is shown in lowercase). Highlighted in teal is the precursor ion that was selected from the inclusion list, and the 4-Da isolation window used for fragmentation is shown in yellow. c, the CID fragmentation spectra and the peptide assignment for the 758.87 ion (lowercase n refers to the N-glycosite). Fragment ions that lack the GlcNAc isomix (such as the y4+ and b6+ fragment ions) have narrow isotopic envelopes, whereas fragments including the GlcNAc isomix (such as the y6+ and b8+ fragment ions) show a perturbed isotopic envelope characteristic of the isomix signature.

Mark A. Breidenbach, et al. Mol Cell Proteomics. 2012 June;11(6):M111.015339.
4.
Fig. 1.

Fig. 1. From: Mapping Yeast N-Glycosites with Isotopically Recoded Glycans.

Metabolic incorporation of a GlcNAc isomix into yeast N-glycans. a, the dibromide triplet pattern, with a 1:2:1 relative peak intensity distribution, results from the natural abundances of 79Br and 81Br isotope pairings. b, a three-component GlcNAc isomix mimics the 1:2:1 peak intensity distribution of dibromide by adjusting the concentration of each synthetically made isotopolog. c, the GlcNAc isomix enters the gna1Δ yeast hexosamine biosynthetic pathway via a heterologous salvage pathway (33). The isomix signature is subsequently embedded into UDP-GlcNAc and any glycoconjugates that utilize UDP-GlcNAc in their construction, including the structurally conserved cores of N-glycans. Following cell lysis, proteolysis, partial enrichment of N-glycopeptides, and partial deglycosylation with endoglycosidase H, the distinctive isotopic signatures of N-glycopeptides are detected computationally using pattern-matching software (25). Masses of putative N-glycopeptide ions are granted fragmentation priority in subsequent LC-MS/MS analyses for N-glycosite identification. The N-glycan precursor illustrated here is composed of two core GlcNAc residues (blue squares), nine mannose residues (green circles), and three glucose residues (blue circles).

Mark A. Breidenbach, et al. Mol Cell Proteomics. 2012 June;11(6):M111.015339.

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