This collection includes both ASU Theses and Dissertations, submitted by graduate students, and the Barrett, Honors College theses submitted by undergraduate students. 

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Protein crystallization is a technique for the formation of three-dimensional protein crystals, which is widely utilized by scientists, engineers, and researchers. Protein crystallography allows for protein structures and functions to be studied. As proteins play a central role in biological systems and life itself, a deeper understanding of their structure-function

Protein crystallization is a technique for the formation of three-dimensional protein crystals, which is widely utilized by scientists, engineers, and researchers. Protein crystallography allows for protein structures and functions to be studied. As proteins play a central role in biological systems and life itself, a deeper understanding of their structure-function properties is crucial to elucidating fundamental behaviors, such as protein folding in addition to the role that they play in emerging fields, such as, tissue engineering with application to the emerging field of regenerative medicine. However, a significant limitation toward achieving further advancements in this field is that in order to determine detailed structure of proteins from protein crystals, high-quality and larger size protein crystals are needed. Because it is difficult to produce adequate size, high-quality crystals, it remains difficult to determine the structure of many proteins. However, a new method using a microgravity environment to crystallize proteins has proven effective through various studies conducted on the International Space Station (ISS). In the presence of microgravity, free convection is essentially absent in the bulk solution where crystallization occurs, thus allowing for purely random Brownian motion to exist which favors the nucleation and growth of high-quality protein crystals. Many studies from the ISS to date have demonstrated that growing protein crystals in a microgravity environment produces larger and higher-quality crystals. This method provides new opportunities for better structure identification and analysis of proteins. Although there remains many more limitations and challenges in the field, microgravity protein crystallization holds many opportunities for the future of biotechnology and scientific development. The objective of this thesis was to study the crystallization of hen egg white lysozyme (HEWL) and determine the effects of both unit and microgravity on growth/size and quality of HEWL. Through preliminary trials using a universal ground-based reduced-gravity system, the crystallization of HEWL in a simulated microgravity environment was successfully conducted and the results reported are promising. The utility of continuous, scalable ground-based, microgravity platforms for studies on a wide range of material systems and behavior, such as, protein crystallization, has significant implications regarding its impact on many industries, including drug development as well as regenerative medicine.
ContributorsTran, Amanda Marie (Author) / Pizziconi, Vincent (Thesis director) / Alford, Terry (Committee member) / Chemical Engineering Program (Contributor) / Barrett, The Honors College (Contributor)
Created2020-12
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Description
This work demonstrates a capable reverse pulse deposition methodology to influence gap fill behavior inside microvia along with a uniform deposit in the fine line patterned regions for substrate packaging applications. Interconnect circuitry in IC substrate packages comprises of stacked microvia that varies in depth from 20µm to 100µm with

This work demonstrates a capable reverse pulse deposition methodology to influence gap fill behavior inside microvia along with a uniform deposit in the fine line patterned regions for substrate packaging applications. Interconnect circuitry in IC substrate packages comprises of stacked microvia that varies in depth from 20µm to 100µm with an aspect ratio of 0.5 to 1.5 and fine line patterns defined by photolithography. Photolithography defined pattern regions incorporate a wide variety of feature sizes including large circular pad structures with diameter of 20µm - 200µm, fine traces with varying widths of 3µm - 30µm and additional planar regions to define a IC substrate package. Electrodeposition of copper is performed to establish the desired circuit. Electrodeposition of copper in IC substrate applications holds certain unique challenges in that they require a low cost manufacturing process that enables a void-free gap fill inside the microvia along with uniform deposition of copper on exposed patterned regions. Deposition time scales to establish the desired metal thickness for such packages could range from several minutes to few hours. This work showcases a reverse pulse electrodeposition methodology that achieves void-free gap fill inside the microvia and uniform plating in FLS (Fine Lines and Spaces) regions with significantly higher deposition rates than traditional approaches. In order to achieve this capability, systematic experimental and simulation studies were performed. A strong correlation of independent parameters that govern the electrodeposition process such as bath temperature, reverse pulse plating parameters and the ratio of electrolyte concentrations is shown to the deposition kinetics and deposition uniformity in fine patterned regions and gap fill rate inside the microvia. Additionally, insight into the physics of via fill process is presented with secondary and tertiary current simulation efforts. Such efforts lead to show “smart” control of deposition rate at the top and bottom of via to avoid void formation. Finally, a parametric effect on grain size and the ensuing copper metallurgical characteristics of bulk copper is also shown to enable high reliability substrate packages for the IC packaging industry.
ContributorsGanesan, Kousik (Author) / Tasooji, Amaneh (Thesis advisor) / Manepalli, Rahul (Committee member) / Alford, Terry (Committee member) / Chan, Candace (Committee member) / Arizona State University (Publisher)
Created2018