Abstract
Three-helix bundle proteins can be assembled by metal driven association of bipyridine-modified peptides. The metal tris-bipyridine complex offers four different templates on which three helices may be arranged to form a bundle structure. Analysis of one of such proteins by HPLC, NMR, and CD shows that all four templates are used randomly. Therefore, this artificial protein does not have a single well defined tertiary structure, but, instead, exists as an ensemble of at least four closely related structures. Mutant peptides with diversified interior residues did not form a stable three-α-helix bundle protein. Packing interactions of interior hydrophobic residues must be optimized to construct artificial proteins with a well defined tertiary structure. This system not only permits us to study packing interactions of secondary structures in artificial proteins but also offers a unique model system for a molten globule state of native proteins.
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