Apoprotein Intermolecular Interactions and Heme Insertion for 3D Domain Swapping in Myoglobin.

ABSTRACT: Many proteins, including heme proteins undergo three-dimensional domain swapping (3D-DS). The loop between E and F helices is converted to a helical structure in the myoglobin (Mb) 3D-DS dimer. However, the relationship between 3D-DS and heme insertion in Mb remains unclear. Here, we systematically investigated the 3D-DS propensity of wild-type (WT) Mb and its variant in which one to three Ala residues were introduced into the hinge region: G80A (K₃AH₂), G80A/H81A (K₃A₂H), and G80A/H81A/H82A (K₃A₃). After heating the Mb monomer at 70 °C for 30 min, no dimers were detected for WT Mb, whereas dimers were formed by 55 ± 1%, 92 ± 2%, and 84 ± 2% of the protein molecules for the K₃AH₂, K₃A_2</

SUBMITTER: Novientri G 

PROVIDER: S-EPMC11865968 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature