Conformational dynamics of a multidomain protein by neutron scattering and computational analysis.

The flexible conformations of a multidomain protein are responsible for its biological functions. Although MurD, a 47-kDa protein that consists of three domains, sequentially changes its domain conformation from an open form to a closed form through a semiclosed form in its enzymatic reaction, the domain dynamics in each conformation remains unclear. In this study, we verify the conformational dynamics of MurD in the corresponding three states (apo and ATP- and inhibitor-bound states) with a combination of small-angle x-ray and neutron scattering (SAXS and SANS), dynamic light scattering (DLS), neutron backscattering (NBS), neutron spin echo (NSE) spectroscopy, and molecular dynamics (MD) simulations.

Site occupancy of interstitial deuterium atoms in face-centred cubic iron.

Hydrogen composition and occupation state provide basic information for understanding various properties of the metal-hydrogen system, ranging from microscopic properties such as hydrogen diffusion to macroscopic properties such as phase stability. Here the deuterization process of face-centred cubic Fe to form solid-solution face-centred cubic FeDx is investigated using in situ neutron diffraction at high temperature and pressure. In a completely deuterized specimen at 988 K and 6.