Fig. 2
From: Dissecting the conformation of glycans and their interactions with proteins
Effects of glycan compositions of SPARC from different sources on binding to collagen I. Analyses of the N-glycopeptide VCSNDN116CFKTFDSSCHFFATK (AA 111–129) of SPARCs from 293 T-WT cells, 293 T-Fut8KO cells and platelets were performed using LC-MS/MS with electron-transfer/higher-energy collision dissociation (EThCD) techniques and Byonic software. EThCD-MS/MS spectra assignments for the b and y fragment ions from the peptide backbone were observed and annotated, which could be used for the sequencing of the peptide. Peptide sequences are depicted in the top right corners. The dissociation with high energy resulted in specific glycan oxonium ions derived from the fragmentation of the N-linked GlcNAc. The summary of peak assignments was shown. a Information for each glycoform in N116 of SPARC, including the m/z of glycosylation, glycan species, and structural composition are depicted. b Biacore analysis of the binding of SPARC from different sources to collagen I. SPARC (1 μM) from 293 T-WT cells (red), 293 T-Fut8KO cells (green), and human platelets (purple), was injected onto separate collagen I-coated sensor chips