Memory Hierarchy Hardware-Software Co-design in Embedded Systems

The memory hierarchy is the main bottleneck in modern computer systems as the gap between the speed of the processor and the memory continues to grow larger. The situation in embedded systems is even worse. The memory hierarchy consumes a large amount of chip area and energy, which are precious resources in embedded systems. Moreover, embedded systems have multiple design objectives such as performance, energy consumption, and area, etc. Customizing the memory hierarchy for specific applications is a very important way to take full advantage of limited resources to maximize the performance. However, the traditional custom memory hierarchy design methodologies are phase-ordered. They separate the application optimization from the memory hierarchy architecture design, which tend to result in local-optimal solutions. In traditional Hardware-Software co-design methodologies, much of the work has focused on utilizing reconfigurable logic to partition the computation. However, utilizing reconfigurable logic to perform the memory hierarchy design is seldom addressed. In this paper, we propose a new framework for designing memory hierarchy for embedded systems. The framework will take advantage of the flexible reconfigurable logic to customize the memory hierarchy for specific applications. It combines the application optimization and memory hierarchy design together to obtain a global-optimal solution. Using the framework, we performed a case study to design a new software-controlled instruction memory that showed promising potential.

SCAPA (Spacially Addressable Protein Array) – a Novel Protein Array for the Differential Profiling of Ligand-receptor Induced Signalling

While protein microarray technology has been successful in demonstrating its usefulness for large scale high-throughput proteome profiling, performance of antibody/antigen microarrays has been only moderately productive. Immobilization of either the capture antibodies or the protein samples on solid supports has severe drawbacks. Denaturation of the immobilized proteins as well as inconsistent orientation of antibodies/ligands on the arrays can lead to erroneous results. This has prompted a number of studies to address these challenges by immobilizing proteins on biocompatible surfaces, which has met with limited success. Our strategy relates to a multiplexed, sensitive and high-throughput method for the screening quantification of intracellular signalling proteins from a complex mixture of proteins. Each signalling protein to be monitored has its capture moiety linked to a specific oligo ‘tag’. The array involves the oligonucleotide hybridization-directed localization and identification of different signalling proteins simultaneously, in a rapid and easy manner. Antibodies have been used as the capture moieties for specific identification of each signaling protein. The method involves covalently partnering each antibody/protein molecule with a unique DNA or DNA derivatives oligonucleotide tag that directs the antibody to a unique site on the microarray due to specific hybridization with a complementary tag-probe on the array. Particular surface modifications and optimal conditions allowed high signal to noise ratio which is essential to the success of this approach.