naa a22 4500 51073846X CHVBK 20180411083019.0 cr unu---uuuuu 180411e20130601xx s 000 0 eng 10.1007/s12127-013-0127-3 doi (NATIONALLICENCE)springer-10.1007/s12127-013-0127-3 Ion mobility-mass correlation trend line separation of glycoprotein digests without deglycosylation [Elektronische Daten] [Hongli Li, Brad Bendiak, William Siems, David Gang, Herbert Hill Jr.] A high-throughput ion mobility mass spectrometer (IMMS) was used to rapidly separate and analyze peptides and glycopeptides derived from glycoproteins. Two glycoproteins, human α-1-acid glycoprotein and antithrombin III were digested with trypsin and subjected to electro-spray traveling wave IMMS analysis. No deglycosylation steps were performed; samples were complex mixtures of peptides and glycopeptides. Peptides and glycosylated peptides with different charge states (up to 4 charges) were observed and fell on distinguishable trend lines in 2-D IMMS spectra in both positive and negative modes. The trend line separation patterns matched between both modes. Peptide sequence was identified based on the corresponding extracted mass spectra and collision induced dissociation (CID) experiments were performed for selected compounds to prove class identification. The signal-to-noise ratio of the glycopeptides was increased dramatically with ion mobility trend line separation compared to non-trend line separation, primarily due to selection of precursor ion subsets within specific mobility windows. In addition, isomeric mobility peaks were detected for specific glycopeptides. IMMS demonstrated unique capabilities and advantages for investigating and separating glycoprotein digests in this study and suggests a novel strategy for rapid glycoproteomics studies in the future. Springer-Verlag Berlin Heidelberg, 2013 Traveling wave ion mobility mass spectrometry nationallicence Glycoprotein nationallicence Peptides nationallicence Glycopeptides nationallicence Mobility-mass trend line separation nationallicence Collision induced dissociation nationallicence Li Hongli Department of Chemistry, Washington State University, Pullman, WA, USA aut Bendiak Brad Department of Cell and Developmental Biology, Program in Structural Biology and Biophysics, University of Colorado, Health Sciences Center, Anschutz Medical Campus, Aurora, CO, USA aut Siems William Department of Chemistry, Washington State University, Pullman, WA, USA aut Gang David Institute of Biological Chemistry, Washington State University, Pullman, WA, USA aut Hill Jr. Herbert Department of Chemistry, Washington State University, Pullman, WA, USA aut International Journal for Ion Mobility Spectrometry Springer-Verlag 16/2(2013-06-01), 105-115 1435-6163 16:2<105 2013 16 12127 https://doi.org/10.1007/s12127-013-0127-3 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s12127-013-0127-3 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Li Hongli Department of Chemistry, Washington State University, Pullman, WA, USA aut NATIONALLICENCE 700 1- Bendiak Brad Department of Cell and Developmental Biology, Program in Structural Biology and Biophysics, University of Colorado, Health Sciences Center, Anschutz Medical Campus, Aurora, CO, USA aut NATIONALLICENCE 700 1- Siems William Department of Chemistry, Washington State University, Pullman, WA, USA aut NATIONALLICENCE 700 1- Gang David Institute of Biological Chemistry, Washington State University, Pullman, WA, USA aut NATIONALLICENCE 700 1- Hill Jr Herbert Department of Chemistry, Washington State University, Pullman, WA, USA aut NATIONALLICENCE 773 0- International Journal for Ion Mobility Spectrometry Springer-Verlag 16/2(2013-06-01), 105-115 1435-6163 16:2<105 2013 16 12127 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer