Abstract
Although increasingly popular, software component techniques still lack suitable formal foundations on top of which rigorous methodologies for the description and analysis of software architectures could be built. This paper aims to contribute in this direction: building on previous work by the authors on coalgebraic semantics, it discusses component refinement at three different but interrelated levels: behavioural, syntactic, i.e., relative to component interfaces, and architectural. Software architectures are defined through component aggregation. On the other hand, such aggregations, no matter how large and complex they are, can also be dealt with as components themselves, which paves the way to a discipline of hierarchical design. In this context, a major contribution of this paper is the introduction of a set of rules for architectural refinement.

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We introduce the concept of identity based key encapsulation to multiple parties (mID-KEM), and define a security model for it. This concept is the identity based analogue of public key KEM to multiple parties. We also analyse possible mID-KEM constructions, and propose an efficient scheme based on bilinear pairings. We prove our scheme secure in the random oracle model under the Gap Bilinear Diffie-Hellman assumption.

Abstract
An increasingly important design constraint for software running on ubiquitous computing devices is security, particularly against physical methods such as side-channel attack. One well studied methodology for defending against such attacks is the concept of indistinguishable functions which leak no information about program control flow since all execution paths are computationally identical. However, constructing such functions by hand becomes laborious and error prone as their complexity increases. We investigate techniques for automating this process and find that effective solutions can be constructed with only minor amounts of computational effort.

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One way of exploring protein unfolding events associated with the development of Amyloid diseases is through the use of multiple Molecular Dynamics Protein Unfolding Simulations. The analysis of the huge amount of data generated in these simulations is not a trivial task. In the present report, we demonstrate the use of Association Rules applied to the analysis of the variation profiles of the Solvent Accessible Surface Area of the 127 amino-acid residues of the protein Transthyretin, along multiple simulations. This allowed us to identify a set of 28 hydrophobic residues forming a hydrophobic cluster that might be essential in the unfolding and folding processes of Transthyretin.