ASU Scholarship Showcase

The following literature review talks about the driving simulation platforms commercially available for automated vehicle development. It is also a comparison of the simulation packages, their advantages and drawbacks, and an insight into what is missing in the simulators of today. Automated vehicle safety and reliability are the important requirements when developing automated vehicles. These requirements are guaranteed by extensive functional and performance tests. Conducting these tests on real vehicles is extremely expensive and time consuming, and thus it is necessary to develop a simulation platform to perform these tasks. In most cases, it is difficult for system or algorithm developers in the testing process to evaluate the massive design space. To test any algorithm change, developers need to test a functional module alone, and later setting up a whole physical testing environment that consists of several other modules, leading to enormous testing costs. Fortunately, many of the testing tasks can be accomplished by utilizing simulator. The key to the success of a simulation is how accurately the simulator can simulate the physical reality.

Background: Cysteine sulfenic acid (Cys-SOH) plays important roles in the redox regulation of numerous proteins. As a relatively unstable posttranslational protein modification it is difficult to quantify the degree to which any particular protein is modified by Cys-SOH within a complex biological environment. The goal of these studies was to move a step beyond detection and into the relative quantification of Cys-SOH within specific proteins found in a complex biological setting--namely, human plasma.

Results: This report describes the possibilities and limitations of performing such analyses based on the use of thionitrobenzoic acid and dimedone-based probes which are commonly employed to trap Cys-SOH. Results obtained by electrospray ionization-based mass spectrometric immunoassay reveal the optimal type of probe for such analyses as well as the reproducible relative quantification of Cys-SOH within albumin and transthyretin extracted from human plasma--the latter as a protein previously unknown to be modified by Cys-SOH.

Conclusions: The relative quantification of Cys-SOH within specific proteins in a complex biological setting can be accomplished, but several analytical precautions related to trapping, detecting, and quantifying Cys-SOH must be taken into account prior to pursuing its study in such matrices.