Each protein has a unique pattern of histidine residues on the surface. Thi
s paper describes the design, synthesis, and binding studies of transition
metal complexes to target the surface histidine pattern of carbonic anhydra
se (bovine erythrocyte). When the pattern of cupric ions on a complex match
es the surface pattern of histidines of the protein, strong and selective b
inding can be achieved in aqueous buffer (pH = 7.0). The described method o
f protein recognition is applicable to proteins of known structures. With r
apidly increasing number of solved protein structures, the method has wide
applicability in purification, targeting, and sensing of proteins.