Structural Characterization of O‐ and C‐Glycosylating Variants of the Landomycin Glycosyltransferase LanGT2

The structures of the O‐glycosyltransferase LanGT2 and the engineered, C? C bond‐forming variant LanGT2S8Ac show how the replacement of a single loop can change the functionality of the enzyme. Crystal structures of the enzymes in complex with a nonhydrolyzable nucleotide‐sugar analogue revealed that there is a conformational transition to create the binding sites for the aglycon substrate. This induced‐fit transition was explored by molecular docking experiments with various aglycon substrates.     

Surface Treatment of Polyimide Substrates Using Dielectric Barrier Discharge Reactors Based on L-Shaped Electrodes

Plasma Chemistry and Plasma Processing - Two dielectric barrier discharge reactors, based on L-shaped electrodes, were designed and fabricated for in-line surface treatment of polyimide (PI)...