Anne Imberty

TL;DR: PA-IL is a bacterial lectin from the opportunistic pathogen Pseudomonas aeruginosa and is involved in the recognition of glycoconjugates on human tissues and the glycoclusters obtained were evaluated as ligands of PA-IL and for their potential for competing with its binding to glycosylated surfaces.

TL;DR: Here, lectin titration data of SWNT- and CCG-based biosensors were used to calculate lectin dissociation constants (K(d)) and compare them to the values obtained from the isothermal titration microcalorimetry technique.

TL;DR: The complete BGT structure now provides a basis for detailed modelling of a BGT HMC-DNA ternary complex and a catalytic mechanism for BGT is proposed and residues involved in both DNA binding and in stabilizing a "flipped-out" 5-HMC nucleotide are identified.

TL;DR: The specificity and kinetics of the interaction between the pathogenesis-related group of thaumatin-like proteins (PR5) in higher plants and (1,3)-β-d-glucans have been investigated, and it is indicated that only specific barley PR5 isoforms interact tightly with ( 1,3-β- d- glucans.

TL;DR: Calculations of partial charges indicated that extensive delocalization of charges between the calcium ions, the side chains of the protein‐binding site and the carbohydrate ligand is responsible for the high enthalpy of binding and therefore for the unusually high affinity observed for this unique mode of carbohydrate recognition.