Abstract
Molecular dynamics simulations are performed to study the mechanical dissociation pathways of a wheat germ agglutinin (WGA) dimer under the tensile force exerted by the atomic force microscopy (AFM). We found a dissociation pathway in which both monomer units are elongated and their tertial structures are destroyed before the rupture. The force extension (F-E) curves are found to show successive saw-tooth peaks indicating the stepwise destruction of interactions inside monomer structures. In addition, the interactions at their interfaces are found to be destroyed at the largest force peak. At the rupture where the dimer dissociates completely, a small jump is observed in the F-E curve, which amounts to 70 pN. [DOI: 10.1380/ejssnt.2009.825]
