Structure and Stability of the Insulin Dimer Investigated by Molecular Dynamics Simulation

Mattia Falconi, Maria Teresa Cambria, Antonio Cambria, Alessandro Desideri
2001 Journal of Biomolecular Structure and Dynamics  
Molecular dynamics simulation indicates that the dynamical behaviour of the insulin dimer is asymmetric. Atomic level knowledge of the interaction modes and protein conformation in the solvation state identifies dynamical structures, held by hydrogen bonds that stabilize, mainly in one monomer, the interaction between the chains. Dynamic cross-correlation analysis shows that the two insulin monomers behave asymmetrically and are almost independent. Solvation energy, calculated to evaluate the
more » ... d to evaluate the contribute of each interface residue to the dimer association pattern, well compares with the experimental association state found in protein mutants indicating that this parameter is an important factor to explain the association properties of mutated insulin dimers. 2 Falconi et al. Figure 1: Schematic view of the insulin dimer. The ribbons represent the protein backbones: the β-strand are indicated by arrows while the α-helices by the twisted ribbons. The A and B chains of each monomer are represented in dark and light grey, respectively. The disulfide bridges are indicated by the ball and stick representation and marked with a label showing the residue numbers and the chain names. This picture was produced by using the MolScript v1.4 program (30).
doi:10.1080/07391102.2001.10506705 pmid:11334112 fatcat:n7fccrkagnduvkhmva4uovv6xm