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Area of Science:

  • Protein biochemistry
  • Structural biology
  • Biophysics

Background:

  • Proteins, including heme proteins like myoglobin (Mb), can undergo three-dimensional domain swapping (3D-DS).
  • In Mb, 3D-DS involves the E-F helix loop converting to a helical structure, forming dimers.
  • The precise relationship between 3D-DS and heme insertion in Mb is not fully understood.

Purpose of the Study:

  • To systematically investigate the propensity of wild-type (WT) Mb and its variants to undergo 3D-DS.
  • To explore the impact of introducing alanine (Ala) residues into the hinge region on Mb dimerization.
  • To elucidate the role of apo monomer-dimer equilibrium and protein folding conditions in Mb 3D-DS.

Main Methods:

  • Thermal denaturation experiments at 70 °C for 30 min to induce 3D-DS in WT Mb and Ala variants (G80A, G80A/H81A, G80A/H81A/H82A).
  • Expression and purification of Mb variants from *Escherichia coli* to assess in vivo dimer formation.
  • Reconstitution of apo Mb variants to evaluate dimer formation independent of heme.
  • Molecular dynamics (MD) simulations to analyze structural changes and stabilization at the hinge region.

Main Results:

  • Heating WT Mb monomer did not yield detectable dimers, while Ala variants showed significant dimer formation (55-92%).
  • In vivo expression and apo Mb reconstitution revealed increased dimer ratios in the order WT < K3AH2 < K3A2H < K3A3.
  • The K3A2H Mb dimer showed stabilization via a hydrogen bond network at the hinge.
  • MD studies supported that stabilized α-helices at the hinge region enhance dimer formation in K3A3 Mb.

Conclusions:

  • Mb 3D-DS dimer formation in vivo is dependent on the apo monomer-dimer equilibrium prior to heme insertion.
  • Ala substitutions in the Mb hinge region significantly promote 3D-DS and dimer formation.
  • Protein folding conditions, particularly the stabilization of hinge region helices, play a critical role in influencing Mb 3D-DS propensity.