ASU Electronic Theses and Dissertations
This collection includes most of the ASU Theses and Dissertations from 2011 to present. ASU Theses and Dissertations are available in downloadable PDF format; however, a small percentage of items are under embargo. Information about the dissertations/theses includes degree information, committee members, an abstract, supporting data or media.
In addition to the electronic theses found in the ASU Digital Repository, ASU Theses and Dissertations can be found in the ASU Library Catalog.
Dissertations and Theses granted by Arizona State University are archived and made available through a joint effort of the ASU Graduate College and the ASU Libraries. For more information or questions about this collection contact or visit the Digital Repository ETD Library Guide or contact the ASU Graduate College at gradformat@asu.edu.
Interactions driving the collapse of islet amyloid polypeptide: implications for amyloid aggregation
In this dissertation, I am interested in the special authentication demands of smart devices and about to satisfy the demands. First, I study how the features of smart devices affect user identity authentications. For identity authentication domain, I aim to design a continuous, forge-resistant authentication mechanism that does not interrupt user-device interactions. I propose a mechanism that authenticates user identity based on the user's finger movement patterns. Next, I study a smart-device-specific authentication, proximity authentication, which authenticates whether two devices are in close proximity. For prox- imity authentication domain, I aim to design a user-friendly authentication mechanism that can defend against relay attacks. In addition, I restrict the authenticated distance to the scale of near field, i.e., a few centimeters. My first design utilizes a user's coherent two-finger movement on smart device screen to restrict the distance. To achieve a fully-automated system, I explore acoustic communications and propose a novel near field authentication system.
that has no regular secondary structure, but plays an important role in vasodilation and pain transmission in migraine. Little is known about the structure and dynamics of the monomeric state of CGRP or how CGRP is able to function in the cell, despite the lack of regular secondary structure. This work focuses characterizing the non-local structural and dynamical properties of the CGRP monomer in solution, and understanding how these are affected by the sequence and the solution environment. The unbound, free state of CGRP is measured using a nanosecond laser-pump spectrophotometer, which allows measuring the end-to-end distance (a non-local structural property) and the rate of end-to-end contact formation (intra-chain diffusional dynamics). The data presented in this work show that electrostatic interactions strongly modulate the structure of CGRP, and that peptide-solvent interactions are sequence and charge dependent and can have a significant effect on the internal dynamics of the peptide. In the last few years migraine research has shifted focus to disrupting the CGRP-receptor pathway through the design of pharmacological drugs that bind to either CGRP or its receptor, inhibiting receptor activation and therefore preventing or reducing the frequency of migraine attacks. Understanding what types of intra- and inter-chain interactions dominate in CGRP can help better design drugs that disrupt the binding of CGRP to its receptor.