Structure and stability of the insulin dimer investigated by molecular dynamics simulation

Molecular dynamics simulation indicates that the dynamical behaviour of the insulin dimer is asymmetric. Atomic level knowledge of the interaction mod es and protein conformation in the solvation state identifies dynamical str uctures, held by hydrogen bonds that stabilize, mainly in one monomer, the interaction between the chains. Dynamic cross-correlation analysis shows th at the two insulin monomers behave asymmetrically and are almost independen t. Solvation energy, calculated to evaluate the contribute of each interfac e residue to the dimer association pattern, well compares with the experime ntal association state found in protein mutants indicating that this parame ter is an important factor to explain the association properties of mutated insulin dimers.