Abstract
Individual anomeric protons that are unresolved in the one-dimensional 250-MHz spectra of oligomannosidic glycopeptides can be separated and characterized by two-dimensional J-resolved NMR spectroscopy. Homogeneous preparations of ovalbumin glycopeptides Man6GlcNAc2Asn and Man5GlcNAc2Asn were characterized by chemical methods, conventional proton NMR, and two-dimensional J-resolved NMR. Due to characteristic differences in coupling constants, mannose (J1,2 less than or equal to 2 Hz) and N-acetylglucosamine (J1,2 approximately 9 Hz) anomeric signals of similar chemical shift were readily separated and identified in the two-dimensional spectra. It is shown that two-dimensional J-resolved NMR spectroscopy, in combination with conventional NMR and limited chemical analysis, is a rapid and reliable technique for the determination of glycopeptide primary structure.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
