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. 2020 Mar 25;117(14):7633–7644. doi: 10.1073/pnas.1916498117

Fig. 4.

Fig. 4.

Distinction of membrane glycoproteins bearing short and extended high-mannose type N-glycans. (A) Number of glycosylated proteins (GPs) associated with the membrane of KKU-213A and/or KKU-213AL5 cells. (B) Number of glycosylated sites (glycosites) on the membrane proteins of KKU-213A and KKU-213AL5 that bear short (Man 5 to 6) or extended (Man 7 to 9) high-mannose type glycans. (C) Frequency of positively charged, negatively charged, polar, and nonpolar amino acid residues surrounding high-mannose–bearing glycosylation sites identified in KKU-213A and KKU-213AL5. Concentric axes show percentage of residues per position relative to the total number of sequons identified in each group. HM, high mannose. Circumferential axes show amino acid position relative to the consensus sequence, N-X-S/T. (D) Abundances of high-mannose–bearing glycopeptides as derived from precursor ion peak areas and normalized to the total protein concentration. (E) Stable conformations of Man 5 (structures a–d) and Man 9 (structures e–h) that arise from conformational isomerism about the C6–C7 bond between residues 3 and 4 and between residues 4 and 6, respectively. (F and G) The largest spanning distances measured between two atoms in Man 5 (structure a) and Man 9 (structure e).