;On the Importance of Carbohydrate-Aromatic Interactions for the Molecular Recognition of Oligosaccharides by Proteins: NMR Studies of the Structure and Binding Affinity of AcAMP2-like Peptides with Non-Natural Naphthyl and Fluoroaromatic Residues.
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Chemistry (2005)
;NMR and modeling studies of protein-carbohydrate interactions:synthesis three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides.
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Chembiochem (2004)
The importance of CH/pi interactions to the function of carbohydrate binding proteins
Protein Pept.Lett. (2002)
;NMR investigations of protein-carbohydrate interactions:synthesis on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N',N"-triacetylchitotriose.
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Proteins (2000)
;Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains.
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Chem.Biol. (2000)
Chemically Prepared Hevein Domains: Effect of C-Terminal Truncation and the Mutagenesis of Aromatic Residues on Affinity for Chitin
Protein Eng. (2000)
1H NMR study of the solution structure of AcAMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.
J.Mol.Biol. (1996)
