In recent years a variety of devices for detectingatoms, molecules, ions or other particles present insolution or in the atmosphere have been devised anddeveloped. In this paper, the species being detectedwill be referred to as the analyte. The goal of thedetection procedure is to determine the ambientanalyte concentration (a number per unit volume)

To study the assembly, the movements and the dissociation of large numbers of molecules in a virtual cell, a simulation program, HSIM, has been developed. The simulator is driven using a description of the model system written in a language we have also developed that does not limit the simulation program to a particular model. We present here the simulation of two completely different models: the growth of actin-like filaments in a prokaryotic cell, and the association and dissociation of proteins into large assemblies.

Most proteins fold in vitro under various renaturation conditions and in so doing, they create a gamut of local solvent environments. The conformation dependence of such environments arises since residues are clustered within a large-scale organization and polar and hydrophobic groups have distinctive ways of organizing solvent around themselves, shaping solvation hulls or cavities. Furthermore, the pairwise interactions of the peptide chain are inevitably sensitive to the environments the chain itself is creating [1-3]. This picture underscores what researchers have termed cooperativity, a central feature of the so-called hydrophobic collapse which suggests a concertedness of folding events requiring the participation of distant parts