Architectural digest: Thermodynamic stability and domain structure of a consensus monomeric globin.

ABSTRACT: Artificial proteins representing the consensus of a set of homologous sequences have attracted attention for their increased thermodynamic stability and conserved activity. Here, we applied the consensus approach to a b-type heme-binding protein to inspect the contribution of a dissociable cofactor to enhanced stability and the chemical consequences of creating a generic heme environment. We targeted the group 1 truncated hemoglobin (TrHb1) subfamily of proteins for their small size (∼120 residues) and ease of characterization. The primary structure, derived from a curated set of ∼300 representative sequences, yielded a highly soluble consensus globin (cGlbN) enriched in acidic residues. Optical and NMR spectroscopies revealed high-affinity heme binding in the expected site and in two orie

SUBMITTER: Martinez Grundman JE 

PROVIDER: S-EPMC10432219 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature