The relation of three-dimensional structure to biosynthesis in the N-linked oligosaccharides

1983 ◽  
Vol 61 (9) ◽  
pp. 1067-1078 ◽  
Author(s):  
Jean-Robert Brisson ◽  
Jeremy P. Carver

The three-dimensional structures are presented for representative N-linked oligosaccharides drawn from four major structural classes. The nuclear magnetic resonance evidence leading to these structures is summarized and the conclusions are compared with those obtained from potential energy calculations and from the crystal structures of fragments. The major finding is that the Manα1-3 arm structure is invariant throughout the series, whereas the Manα1-6 arm has two possible orientations in some structures and a single orientation in others. Finally, the three-dimensional structures permit a rationalization of the substrate specificity of several key enzymes in the biosynthetic pathway.

Toxins ◽  
2018 ◽  
Vol 10 (11) ◽  
pp. 437 ◽  
Author(s):  
David Wilson ◽  
Norelle L. Daly

Structural analysis of peptides with nuclear magnetic resonance (NMR) spectroscopy generally relies on knowledge of the primary sequence to enable assignment of the resonances prior to determination of the three-dimensional structure. Resonance assignment without knowledge of the sequence is complicated by redundancy in amino acid type, making complete de novo sequencing using NMR spectroscopy unlikely to be feasible. Despite this redundancy, we show here that NMR spectroscopy can be used to identify short sequence tags that can be used to elucidate full-length peptide sequences via database searching. In the current study, we have used this approach to identify conotoxins from the venom of the cone snail Conus geographus and determined the three-dimensional structure of a member of the I3 superfamily. This approach is most likely to be useful for the characterization of disulfide-rich peptides, such as those that were chosen for this study, as they generally have well-defined structures, which enhances the quality of the NMR spectra. In contrast to other sequencing methods, the lack of sample manipulation, such as protease digestion, allows for subsequent bioassays to be carried out using the native sample used for sequence identification.


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