An infrared source with spatially and temporally variable radiance is designed. It can be used to simulate any other infrared source simultaneously in two wavelength bands. The theoretical analysis of the real and simulator source is performed to define the design parameters. A series of the concepts are evaluated for their potential as infrared sources. A three-dimensional heat transfer computer program is used to predict the thermal behavior of the prototype glassy carbon waffle target. Tests are performed on this target which show that its thermal and radiation properties are in agreement with its predicted behavior. Glassy carbon waffle source is a good infrared radiator which can be used repeatedly at high temperatures. Measurements are described which show that the uniformity in the surface temperature can be maintained even when a scanning laser beam is used to deposit the energy on the target surface. The target surface is described analytically as a low pass filter. Its time constant is shown to depend on the target material and the temperature distribution in the target.

No description available.

No description available.

The defects and fault tolerance study is essential in the QCA devices in order to know its characteristics. Knowing the characteristics, one can understand the flow of information in a QCA system with and without manufacturing and operational defects. The manufacturing defects could be at device level or cell level. At the device level, the cell could be rotated, displaced vertically or horizontally, the cell could be missing or the size of the cell could be different. At the cell level, there could be a missing dot, dot could be displaced from its position or the size of the dots could be different. The operational defects are due to its surrounding, such as temperature or stray charge. Each of these defects and fault tolerances can be studies in detail in order to find the optimum working conditions where the information can be safely transmitted to the appropriate locations in the device.The theoretical studies have shown that at absolute temperature and without any defect, the QCA devices are operational. But it is almost impossible to manufacture a perfect or defect free device, and also it is impractical to think about operating a system at absolute zero temperature environment.Therefore, it is important to investigate the fault tolerant properties with defects and higher temperatures to see how far the QCA device can operate safely. Many studies have been done to investigate the fault tolerant properties in QCA devices. However, these studies have not completely exhausted the study of defects and temperature effects. In this study, the dot displacement and missing dots with temperature effects are investigated for the basic QCA devices and a Full Adder. In order to study fault tolerant properties, the existing theoretical model and computer simulation programs have been expanded and used. The defect characteristics have been simulated using normal distribution. / Department of Physics and Astronomy

No description available.

Graduation date: 1988

Thesis (Ph. D.)--University of Hawaii at Manoa, 1982. / Bibliography: leaves 242-245. / Microfiche. / xiii, 245 leaves, bound ill. 29 cm

Typescript (photocopy).

A project report submitted to the Faculty of Engineering, University of the Witwatersrand, Johannesburg, in partial fulfilment of the requirements for the degree of Master of Science in Engineering. / The simulator uses the Monte Carlo technique to quickly and accurately estimate the reliability and availability of complex network systems, Non-exponential failure and repair distributions are included in the model, as is standby redundancy and K out of N active redundancy. The program is easy to use and will work on a large variety of computers and FORTRAN compilers. Some knowledge of FORTRAN is required to program the simulator for each reliability network, The simulator is limited to the analysis of network systems, i.e, those systems whose logic can be fully represented by a reliability block diagram. The applicability of the model was demonstrated by the analysis of numerous systems in the aerospace and industrial environments. Validation of the model was accomplished by comparing these results with analytically determined values, or those from AMIR and SPAR where an analytic solution was impossible. / Andrew Chakane 2018

Amyloids are highly ordered cross-β sheet aggregates that are associated with many diseases such as Alzheimer‟s, type II diabetes and prion diseases. Recently a progress has been made in structure elucidation, environmental effects and thermodynamic properties of amyloid aggregates. However, detailed understanding of how mutation, packing polymorphism and small organic molecules influence amyloid structure and dynamics is still lacking. Atomistic modeling of these phenomena with molecular dynamics (MD) simulations holds a great promise to bridge this gap. This Thesis describes the results of MD simulations, which provide insight into the effects of mutation, packing polymorphism and molecular inhibitors on amyloid peptides aggregation. Chapter 1 discusses the structure of amyloid peptides, diseases associated with amyloid aggregation, mechanism of aggregation and strategies to treat amyloid diseases. Chapter 2 describes the basic principles of molecular dynamic simulation and methods of trajectory analysis used in the Thesis. Chapter 3 presents the results of the study of several all-atom molecular dynamics simulations with explicit solvent, starting from the crystalline fragments of two to ten monomers each. Three different hexapeptides and their analogs produced with single glycine replacement were investigated to study the structural stability, aggregation behavior and thermodynamics of the amyloid oligomers. Chapter 4 presents multiple molecular dynamics (MD) simulation of a pair polymorphic form of five short segments of amyloid peptide. Chapter 5 describes MD study of single-layer oligomers of the full-length insulin with a goal to identify the structural elements that are important for insulin amyloid stability, and to suggest single glycine mutants that may improve formulation. Chapter 6 presents the investigation of the mechanism of the interaction of polyphenols molecules with the protofibrils formed by an amyloidogenic hexapeptide fragment (VQIVYK) of Tau peptide by molecular dynamics iii simulations in explicit solvent. We analyzed the trajectories of the large (7×4) aggregate with and without the polyphenols. Our MD simulations for both the short and full length amyloids revealed adding strands enhances the internal stability of wildtype aggregates. The degree of structural similarity between the oligomers in simulation and the fibril models constructed based on experimental data may explain why adding oligomers shortens the experimentally observed nucleation lag phase of amyloid aggregation. The MM-PBSA free energy calculation revealed nonpolar components of the free energy is more favorable while electrostatic solvation is unfavorable for the sheet to sheet interaction. This explains the acceleration of aggregation by adding nonpolar co-solvents (methanol, trifluoroethanol, and hexafluoroisopropanol). Free energy decomposition shows residues situated at the interface were found to make favorable contribution to the peptide -peptide association. The results from the simulations might provide both the valuable insight for amyloid aggregation as well as assist in inhibitor design efforts. First, the simulation of the single glycine mutants at the steric zipper of the short segments of various pathological peptides indicates the intersheet steric zipper is important for amyloid stability. Mutation of the side chains at the dry steric zipper disrupts the sheet to sheet packing, making the aggregation unstable. Thus, designing new peptidomimetic inhibitors able to prevent the fibril formation based on the steric zipper motif of the oligomers, similar to the ones examined in this study may become a viable therapeutic strategy. The various steric zipper microcrystal structures of short amyloid segments could be used as a template to design aggregation inhibitor that can block growth of the aggregates. Modification of the steric zipper structure (structure based design) with a single amino acid changes, shuffling the sequences, N- methylation of peptide amide bonds to suppress hydrogen iv bonding ability of NH groups or replacement with D amino acid sequence that interact with the parent steric zipper could be used in computational search for the new inhibitors. Second, the polyphenols were found to interact with performed oligomer through hydrogen bonding and induce conformational change creating an altered aggregate. The conformational change disrupts the intermolecular amyloid contact remodeling the amyloid aggregate. The recently reported microcrystal structure of short segments of amyloid peptides with small organic molecules could serve as a pharamcophore for virtual screening of aggregation inhibitor using combined docking and MD simulation with possible enhancement of lead enrichment. Finally, our MD simulation of short segments of amyloids with steric zipper polymorphism showed the stability depends on both sequence and packing arrangements. The hydrophilic polar GNNQQNY and NNQNTF with interface containing large polar and/or aromatic side chains (Q/N) are more stable than steric zipper interfaces made of small or hydrophobic residues (SSTNVG, VQIVYK, and MVGGVV). The larger sheet to sheet interface of the dry steric zipper through polar Q/N rich side chains was found to holds the sheets together better than non Q/N rich short amyloid segments. The packing polymorphism could influence the structure based design of aggregation inhibitor and a combination of different aggregation inhibitors might be required to bind to various morphologic forms of the amyloid peptides.