We have developed a robust platform to transpose metalloprotein coordination into porous crystalline materials. Though only a small fraction of possible sequences have been explored, some of these frameworks already show coordination environments found in many important metalloproteins. Our strategy leverages stabilized short ɑ-helices 9 amino acids long, decorated with metal-binding groups (MAHFs), which form numerous unique metal-peptide frameworks through the synergy of coordination bonds, hydrophobic van der Waals interactions, and H-bonding. This finding significantly expands the field of metal-peptide frameworks by providing a convenient, reliable, and versatile method to make highly crystalline frameworks with site-isolated metal centers that are coordinated by the common residues found in most metalloproteins. Most importantly, these MAHFs allow for many variations. Tuning a secondary sphere residue produces an enormous range of coordination spheres. Mutating a position to all 20 canonical amino acids still produces crystalline materials, showcasing the robustness of the framework design. Furthermore, a range of transition metals can be used. Combined with the ease of their synthesis, metal-ɑ -helix frameworks could be highly versatile scaffolds for exploring bioinorganic model systems. In this report, only one position of the helix was varied, but there are numerous avenues for framework engineering, including variation of the other packing positions, design of the metal-binding motifs, and peptide length. Though the mutations here mostly result in a novel topology, it will be of interest to target more framework topologies that are robust towards mutations, which would allow subtle secondary sphere or pore engineering around a metal site without perturbing its primary sphere coordination. The nearly isostructural series of A8, A8G, and A8F series with Co(II) demonstrates that such mutational robustness is possible. Another opportunity for exploration involves framework synthesis with metal ions with different oxidation states.