2 resultados para X-ray computed tomography
em Illinois Digital Environment for Access to Learning and Scholarship Repository
Resumo:
Open-cell metal foams show promise as an emerging novel material for heat exchanger applications. The high surface-area-to-volume ratio suggests increased compactness and decrease in weight of heat exchanger designs. However, the metal foam structure appears conducive to condensate retention, which would degenerate heat transfer performance. This research investigates the condensate retention behavior of aluminum open-cell metal foams through the use of static dip tests and geometrical classification via X-ray Micro-Computed Tomography. Aluminum open-cell metal foam samples of 5, 10, 20, and 40 pores per inch (PPI), all having a void fraction greater than 90%, were included in this investigation. In order to model the condensate retention behavior of metal foams, a clearer understanding of the geometry was required. After exploring the ideal geometries presented in the open literature, X-ray Micro-Computed Tomography was employed to classify the actual geometry of the metal foam samples. The images obtained were analyzed using specialized software from which geometric information including strut length and pore shapes were extracted. The results discerned a high variability in ligament length, as well as features supporting the ideal geometry known as the Weaire-Phelan unit cell. The static dip tests consisted of submerging the metal foam samples in a liquid, then allowing gravity-induced drainage until steady-state was reached and the liquid remaining in the metal foam sample was measured. Three different liquids, water, ethylene glycol, and 91% isopropyl alcohol, were employed. The behaviors of untreated samples were compared to samples subjected to a Beomite surface treatment process, and no significant differences in retention behavior were discovered. The dip test results revealed two distinct regions of condensate retention, each holding approximately half of the total liquid retained by the sample. As expected, condensate retention increased as the pores sizes decreased. A model based on surface tension was developed to predict the condensate retention in the metal foam samples and verified using a regular mesh. Applying the model to both the ideal and actual metal foam geometries showed good agreement with the dip test results in this study.
Resumo:
The protein folding problem has been one of the most challenging subjects in biological physics due to its complexity. Energy landscape theory based on statistical mechanics provides a thermodynamic interpretation of the protein folding process. We have been working to answer fundamental questions about protein-protein and protein-water interactions, which are very important for describing the energy landscape surface of proteins correctly. At first, we present a new method for computing protein-protein interaction potentials of solvated proteins directly from SAXS data. An ensemble of proteins was modeled by Metropolis Monte Carlo and Molecular Dynamics simulations, and the global X-ray scattering of the whole model ensemble was computed at each snapshot of the simulation. The interaction potential model was optimized and iterated by a Levenberg-Marquardt algorithm. Secondly, we report that terahertz spectroscopy directly probes hydration dynamics around proteins and determines the size of the dynamical hydration shell. We also present the sequence and pH-dependence of the hydration shell and the effect of the hydrophobicity. On the other hand, kinetic terahertz absorption (KITA) spectroscopy is introduced to study the refolding kinetics of ubiquitin and its mutants. KITA results are compared to small angle X-ray scattering, tryptophan fluorescence, and circular dichroism results. We propose that KITA monitors the rearrangement of hydrogen bonding during secondary structure formation. Finally, we present development of the automated single molecule operating system (ASMOS) for a high throughput single molecule detector, which levitates a single protein molecule in a 10 µm diameter droplet by the laser guidance. I also have performed supporting calculations and simulations with my own program codes.