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Ligand‐Directed Immobilization of Proteins through an Esterase 2 Fusion Tag Studied by Atomic Force Microscopy

Atomically flat mica surfaces were chemically modified with an alkyl trifluoromethyl ketone, a covalent inhibitor of esterase 2 from Alicyclobacillus acidocaldarius, which served as a tag for ligand‐directed immobilization of esterase‐linked proteins. Purified NADH oxidase from Thermus thermophilus and human exportin‐t from cell lysates were anchored on the modified surfaces. The immobilization effectiveness of the proteins was studied by atomic force microscopy (AFM). It was shown that ligand–esterase interaction allowed specific attachment of exportin‐t and resulted in high‐resolution images and coverage patterns that were comparable with immobilized purified protein. Moreover, the biological functionality of immobilized human exportin‐t in forming a quaternary complex with tRNA and the GTPase Ran‐GTP, and the dimension changes before and after complex formation were also determined by AFM.