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Gewählte Publikation:

Bindila, L; Steiner, K; Schäffer, C; Messner, P; Mormann, M; Peter-Katalinic, J.
(2007): Sequencing of O-glycopeptides derived from an S-layer glycoprotein of Geobacillus stearothermophilus NRS 2004/3a containing up to 51 monosaccharide residues at a single glycosylation site by fourier transform ion cyclotron resonance infrared multiphoton dissociation mass spectrometry.
Anal Chem. 2007; 79(9):3271-3279 FullText FullText_BOKU

The microheterogeneity of large sugar chains in glycopeptides from S-layer glycoproteins containing up to 51 monosaccharide residues at a single O-attachment site on a 12 amino acid peptide backbone was investigated by Fourier transform ion cyclotron resonance mass spectrometry (FTICR MS). Structural elucidation of glycopeptides with the same amino acid sequence and different glycoforms, having such a high saccharide-to-peptide ratio, was achieved by applying infrared multiphoton dissociation (IRMPD) MS/MS for the first time. A 100% sequence coverage of the glycan chain and a 50% coverage of the peptide backbone fragmentation were obtained. The microheterogeneity of carbohydrate chains at the same glycosylation site, containing largely rhamnose, could have been reliably assessed.
Autor*innen der BOKU Wien:
Messner Paul
Schäffer Christina
Find related publications in this database (using NML MeSH Indexing)
Amino Acid Sequence -
Bacillus stearothermophilus - chemistry
Bacterial Proteins - chemistry
Carbohydrate Sequence -
Fourier Analysis -
Glycopeptides - analysis
Glycosylation -
Mass Spectrometry - instrumentation
Membrane Glycoproteins - chemistry
Molecular Sequence Data -
Monosaccharides - chemistry
Sensitivity and Specificity -
Sequence Analysis, Protein - methods

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