Mark R. Wormald

TL;DR: In this study, the current knowledge on FcγR glycosylation is discussed, and some insight into its role and influence on the interaction properties with IgG, particularly in the context of biotherapeutics is provided.

TL;DR: The data presented here suggests that the most likely epitope for 2G12 is formed from a specific cluster of mannose residues on the outer face of gp120, with the other glycans playing an indirect role in maintaining epitope conformation.

TL;DR: A tentative fold for the iron-uptake regulation protein (Fur) from Escherichia coli is put forward, which is seen to have a relatively rigid series of interior strands and more flexible exterior strands, many of which are likely to be helical.

TL;DR: NMR spectroscopy of a 13C-labeled chromopeptide provided indication for broadening due to conformational exchange reactions in the intact photoreceptor domain, which is more pronounced for the C- and D-rings of the chromophore.

TL;DR: An analysis of the released oligosaccharides from a membrane glycoprotein preparation of third instar larvae, and purified larval serum protein 2 from Drosophila melanogaster revealed two series of oligomannosides; one of these series was unusual and characterized by the presence of a core alpha 1-6 linked fucose, and the other was a typical mammalian oligumannose series.