Accurate failure prediction in conjunction with efficient process migration facilities including some Cloud constructs can enable failure avoidance in large-scale high performance computing (HPC) platforms. In this work we demonstrate a prototype system that incorporates our probabilistic failure prediction system with virtualization mechanisms and techniques to provide a whole system approach to failure avoidance. This work utilizes a failure scenario based on a real-world HPC case study.

Statistical analysis is widely used for countless scientific applications in order to analyze and infer meaning from data. A key challenge of any statistical analysis package aimed at large-scale, distributed data is to address the orthogonal issues of parallel scalability and numerical stability. In this paper we derive a series of formulas that allow for single-pass, yet numerically robust, pairwise parallel and incremental updates of both arbitrary-order centered statistical moments and co-moments. Using these formulas, we have built an open source parallel statistics framework that performs principal component analysis (PCA) in addition to computing descriptive, correlative, and multi-correlative statistics. The results of a scalability study demonstrate numerically stable, near-optimal scalability on up to 128 processes and results are presented in which the statistical framework is used to process large-scale turbulent combustion simulation data with 1500 processes.

Using the cloud computing paradigm, a host of companies promise to make huge compute resources available to users on a pay-as-you-go basis. These resources can be configured on the fly to provide the hardware and operating system of choice to the customer on a large scale. While the current target market for these resources in the commercial space is Web development/hosting, this model has the lure of savings of ownership, operation, and maintenance costs, and thus sounds like an attractive solution for people who currently invest millions to hundreds of millions of dollars annually on high performance computing (HPC) platforms in order to support large-scale scientific simulation codes. Given the current interconnect bandwidth and topologies utilized in these commercial offerings, however, the only current viable market in HPC would be small-memory-footprint embarrassingly parallel or loosely coupled applications, which inherently require little to no inter-processor communication. While providing the appropriate resources (bandwidth, latency, memory, etc.) for the HPC community would increase the potential to enable HPC in cloud environments, this would not address the need for scalability and reliability, crucial to HPC applications. Providing for these needs is particularly difficult in commercial cloud offerings where the number of virtual resources can far outstrip the number of physical resources, the resources are shared among many users, and the resources may be heterogeneous. Advanced resource monitoring, analysis, and configuration tools can help address these issues, since they bring the ability to dynamically provide and respond to information about the platform and application state and would enable more appropriate, efficient, and flexible use of the resources key to enabling HPC. Additionally such tools could be of benefit to non-HPC cloud providers, users, and applications by providing more efficient resource utilization in general.

MOTIVATION: Proteome-wide prediction of protein-protein interaction is a difficult and important problem in biology. Although there have been recent advances in both experimental and computational methods for predicting protein-protein interactions, we are only beginning to see a confluence of these techniques. In this paper, we describe a very general, high-throughput method for predicting protein-protein interactions. Our method combines a sequence-based description of proteins with experimental information that can be gathered from any type of protein-protein interaction screen. The method uses a novel description of interacting proteins by extending the signature descriptor, which has demonstrated success in predicting peptide/protein binding interactions for individual proteins. This descriptor is extended to protein pairs by taking signature products. The signature product is implemented within a support vector machine classifier as a kernel function. RESULTS: We have applied our method to publicly available yeast, Helicobacter pylori, human and mouse datasets. We used the yeast and H.pylori datasets to verify the predictive ability of our method, achieving from 70 to 80% accuracy rates using 10-fold cross-validation. We used the human and mouse datasets to demonstrate that our method is capable of cross-species prediction. Finally, we reused the yeast dataset to explore the ability of our algorithm to predict domains. CONTACT: [email protected]

MOTIVATION: Specific and sensitive ligand-based protein detection assays that employ antibodies or small molecules such as peptides, aptamers or other small molecules require that the corresponding surface region of the protein be accessible and that there be minimal cross-reactivity with non-target proteins. To reduce the time and cost of laboratory screening efforts for diagnostic reagents, we developed new methods for evaluating and selecting protein surface regions for ligand targeting. RESULTS: We devised combined structure- and sequence-based methods for identifying 3D epitopes and binding pockets on the surface of the A chain of ricin that are conserved with respect to a set of ricin A chains and unique with respect to other proteins. We (1) used structure alignment software to detect structural deviations and extracted from this analysis the residue-residue correspondence, (2) devised a method to compare corresponding residues across sets of ricin structures and structures of closely related proteins, (3) devised a sequence-based approach to determine residue infrequency in local sequence context and (4) modified a pocket-finding algorithm to identify surface crevices in close proximity to residues determined to be conserved/unique based on our structure- and sequence-based methods. In applying this combined informatics approach to ricin A, we identified a conserved/unique pocket in close proximity (but not overlapping) the active site that is suitable for bi-dentate ligand development. These methods are generally applicable to identification of surface epitopes and binding pockets for development of diagnostic reagents, therapeutics and vaccines.