Modeling of relay helix functional dynamics and feasibility of experimental verification by neutron scattering

Abstract

Cellular long-range transport involves motor proteins (MPs) (especially, kinesin and myosin) which contain a so-called relay helix. Its motion is of crucial importance to the conversion of chemical energy released in ATP hydrolysis into the coordinated mechanical movement of the entire motor protein. In this paper, we propose two combined nonlinear mechanisms for this particular functional activity and suggest the application of neutron scattering assays to experimentally determine the incoherent dynamic structure factor S(q, omega). We argue that this type of experiment is not only feasible but it could offer significant insights into the mechanism of MP function at a molecular level.