Sparse Signal Representation of Ultrasonic Signals for Structural Health Monitoring Applications

Assessment of the integrity of structural components is of great importance for aerospace systems, land and marine transportation, civil infrastructures and other biological and mechanical applications. Guided waves (GWs) based inspections are an attractive mean for structural health monitoring. In this thesis, the study and development of techniques for GW ultrasound signal analysis and compression in the context of non-destructive testing of structures will be presented. In guided wave inspections, it is necessary to address the problem of the dispersion compensation. A signal processing approach based on frequency warping was adopted. Such operator maps the frequencies axis through a function derived by the group velocity of the test material and it is used to remove the dependence on the travelled distance from the acquired signals. Such processing strategy was fruitfully applied for impact location and damage localization tasks in composite and aluminum panels. It has been shown that, basing on this processing tool, low power embedded system for GW structural monitoring can be implemented. Finally, a new procedure based on Compressive Sensing has been developed and applied for data reduction. Such procedure has also a beneficial effect in enhancing the accuracy of structural defects localization. This algorithm uses the convolutive model of the propagation of ultrasonic guided waves which takes advantage of a sparse signal representation in the warped frequency domain. The recovery from the compressed samples is based on an alternating minimization procedure which achieves both an accurate reconstruction of the ultrasonic signal and a precise estimation of waves time of flight. Such information is used to feed hyperbolic or elliptic localization procedures, for accurate impact or damage localization.

Structural and biochemical studies of Sporosarcina pasteurii UreE: a nickel-chaperone involved in the urease activation process

Urease is a nickel-dependent enzyme that catalyzes hydrolysis of urea in the last step of organic nitrogen mineralization. Its active site contains a dinuclear center for Ni(II) ions that must be inserted into the apo-enzyme through the action of four accessory proteins (UreD, UreE, UreF, UreG) leading to activation of urease. UreE, acting as a metallo-chaperone, delivers Ni(II) to the preformed complex of apo-urease-UreDFG and has the capability to enhance the GTPase activity of UreG. This study, focused on characterization of UreE from Sporosarcina pasteurii (SpUreE), represents a piece of information on the structure/mobility-function relationships that control nickel binding by SpUreE and its interaction with SpUreG. A calorimetric analysis revealed the occurrence of a binding event between these proteins with positive cooperativity and a stoichiometry consistent with the formation of the (UreE)2-(UreG)2 hetero-oligomer complex. Chemical Shift Perturbations induced by the protein-protein interaction were analyzed using high-resolution NMR spectroscopy, which allowed to characterize the molecular details of the protein surface of SpUreE involved in the complex formation with SpUreG. Moreover, backbone dynamic properties of SpUreE, determined using 15N relaxation analysis, revealed a general mobility in the nanoseconds time-scale, with the fastest motions observed at the C-termini. The latter analysis made it possible for the first time to characterize of the C-terminal portions, known to contain key residues for metal ion binding, that were not observed in the crystal structure of UreE because of disorder. The residues belonging to this portion of SpUreE feature large CSPs upon addition of SpUreG, showing that their chemical environment is directly affected by protein-protein interaction. Metal ion selectivity and affinity of SpUreE for cognate Ni(II) and non cognate Zn(II) metal ions were determined, and the ability of the protein to select Ni(II) over Zn(II), in consistency with the proposed role in Ni(II) cations transport, was established.