Changes in glycosylation have long been associated with disease. While there are many methods to detect changes in glycosylation, plant derived lectins are often used to determine changes on specific proteins or molecules of interest. One change in glycosylation that has been observed by us and by others is a disease or antigen associated increase in fucosylation on N-linked glycans. To measure this change, the fucose binding Aleuria aurantia lectin (AAL) is often utilized in plate and solution based assays. AAL is a mushroom derived lectin that contains five fucose binding sites that preferentially bind fucose linked (α-1,3, α-1,2, α-,4, and α-1,6) to N-acetyllactosamine related structures. Recently, several reports by us and by others have indicated that specific fucose linkages found on certain serum biomarker glycoprotein's are more associated with disease than others. Taking a site-directed mutagenesis approach, we have created a set of recombinant AAL proteins that display altered binding affinities to different analytes containing various fucose linkages.

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Raman spectroscopy has been used in a qualitative analysis of iron containing lithium silicate glasses. The iron was kept fixed at 8 mol% for all the iron containing samples with varying concentrations of Li2O and SiO2, as this resulted in samples that were fully vitreous in nature. The method of deconvolution of peaks in these data has been employed to understand the relative numbers of Q0, Q1, Q2, Q3, and Q4 silicate structural units. Even though the iron concentration is constant, the linkages of silicate structural units show variation with increasing alkali content. The roles of lithium and iron have been found to be opposed to each other in that the presence of lithium discourages formation of tetrahedral linkages in the structure, whereas iron promotes corner connected tetrahedra or the presence of bridging oxygens.