Cyclic Deformation Induced Residual Stress Evolution and 3D Short Fatigue Crack Growth Investigated by Advanced Synchrotron Tomography Techniques.

Diffraction and phase contrast tomography techniques were successfully applied to an austenitic-ferritic duplex stainless steel representing exemplarily a metallic material containing two phases with different crystal structures. The reconstructed volumes of both phases were discretized by finite elements. A crystal plasticity finite-element analysis was executed in order to simulate the development of the experimentally determined first and second order residual stresses, which built up due to the manufacturing process of the material. Cyclic deformation simulations showed the single-grain-resolved evolution of initial residual stresses in both phases and were found to be in good agreement with the experimental results. Solely in ferritic grains, residual stresses built up due to cyclic deformation, which promoted crack nucleation in this phase. Furthermore, phase contrast tomography was applied in order to analyze the mechanisms of fatigue crack nucleation and short fatigue crack propagation three-dimensionally and nondestructively. The results clearly showed the significance of microstructural barriers for short fatigue crack growth at the surface, as well as into the material. The investigation presented aims for a better understanding of the three-dimensional mechanisms governing short fatigue crack propagation and, in particular, the effect of residual stresses on these mechanisms. The final goal was to generate tailored microstructures for improved fatigue resistance and enhanced fatigue life.

Subsurface influence on the structure of protein adsorbates as revealed by in situ X-ray reflectivity.

The adsorption process of proteins to surfaces is governed by the mutual interactions among proteins, the solution, and the substrate. Interactions arising from the substrate are usually attributed to the uppermost atomic layer. This actual surface defines the surface chemistry and hence steric and electrostatic interactions. For a comprehensive understanding, however, the interactions arising from the bulk material also have to be considered. Our protein adsorption experiments with globular proteins (α-amylase, bovine serum albumin, and lysozyme) clearly reveal the influence of the subsurface material via van der Waals forces. Here, a set of functionalized silicon wafers enables a distinction between the effects of surface chemistry and the subsurface composition of the substrate. Whereas the surface chemistry controls whether the individual proteins are denatured, the strength of the van der Waals forces affects the final layer density and hence the adsorbed amount of proteins. The results imply that van der Waals forces mainly influence surface processes, which govern the structure formation of the protein adsorbates, such as surface diffusion and spreading.

Effect of urea and glycerol on the adsorption of ribonuclease A at the air-water interface.

This study reports on the influence of nonionic cosolvents on the interfacial structure of ribonuclease A (RNase) adsorbed at the air-water interface. We applied X-ray reflectometry to obtain detailed volume fraction profiles of the adsorbed layers and to follow the effect of glycerol and urea on the adsorbate structure as a function of cosolvent concentration. Under all conditions studied, the adsorbed RNase layer maintains its compact shape, and the adsorbed RNase molecules adopt a flat-on orientation at the interface. Both kosmotropic glycerol and chaotropic urea exert profound effects on the adsorbate: The surface excess decreases linearly with glycerol content and is also reduced at low urea concentration. However, at high urea concentration, parts of the adsorbed layer are dehydrated and become exposed to air. The electron density and volume fraction profiles of the adsorbed protein provide clear evidence that these effects are ruled by different mechanisms.