Amino Acid Sequence Design of the Hinge Region in DomainSwapping for Construction of Protein Supramolecules

摘要

Myoglobin (Mb) is a monomeric hemoprotein possessing eight α-helices,andfunctions as an oxygen storage protein.We have previously shown that Mb can form adomain-swapped dimer by treatment with ethanol.1,2 Based on the structural change of thehinge region from a loop to an α-helical structure upon dimerization of Mb,we designedstable Mb dimers by modifying the amino acid sequence of the hinge region.We alsoconstructed Mb mutants which can form dimers with metal binding ability.