The role of protein Z (PZ) in the etiology of human disorders is unclear. A number of PZ gene variants, sporadic or polymorphic and found exclusively in the serine protease domain, have been observed. Crystal structures of PZ in complex with the PZ-dependent inhibitor (PZI) have been recently obtained. The aim of this study was a structural investigation of the serine protease PZ domain, aiming at finding common traits across disease-linked mutations. We performed 10-20 ns molecular dynamics for each of the observed PZ mutants to investigate their structure in aqueous solution.

The first part of this work reviews the algebraic matricial approach to transport data inversion. It works for the convection-diffusion transport equation used for periodic signals and provides a formally exact solution, as well as a quantitative assessment of error bars. The standard methods of reconstruction infer the diffusivity D and pinch V by matching experimental data against those simulated by transport codes. These methods do not warrant the validity of either the underlying models of transport, or of the reconstructed D(r) and V(r), even when the results look reasonable.

The results of accurate compressible Navier-Stokes simulations of aerodynamic heating of the Vega launcher are presented. Three selected steady conditions of the Vega mission profile are considered: the first corresponding to the altitude of 18 km, the second to 25 km and the last to 33 km. The numerical code is based on the mathematical model described by the Favre-Average-Navier-Stokes equations; the turbulent model chosen for closure is the one-equation model by Spalart-Allmaras.