Many companies have adopted some form of environmental programme to manage their relationship with nature. However, a company's environmental achievements tend to be disconnected from its general operations; consequently, these achievements are ineffective. The purpose of this article is to employ a conceptual approach to explore ways to compose effective corporate environmental strategies. From a resource perspective, the flow of material, knowledge and experiences, relationships, communication, and cooperation and control are discussed as strategy aspects central to an effective environmental strategy. Using these five strategy aspects we show how three different strategies with different contents and directions can be assembled. Copyright © 2014 John Wiley & Sons, Ltd and ERP Environment

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A dream of many pharmaceutical companies is to be able to register a large design space with the regulatory agencies. The problem is that this will require both time and money, so an intelligent method of validating a design space is needed. The design space should only cover operating points at which the process runs optimally. This means that the process should be optimized for different process scenarios and objective functions and the found operating points should be registered as design space. This paper presents a method of determining a good design space by creating Pareto fronts for the ideal case and for various process disturbance scenarios. Optimal operating points are found for varying ratios between feed costs and operating costs, making it possible to make a quantitative choice of an operating point based on this ratio and a qualitative choice based on the whole front. The analysis will show how the chromatographic process can be made more robust when optimizing for higher yields, and how the effect of the critical process parameters can change. To be certain that a robust process is found and that it has a high performance, process disturbances must be taken into account when optimizing a process.

Proteins possess a complex and dynamic structure, which is influenced by external signals and may change as they perform their biological functions. We present an optical approach, distance-encoding photoinduced electron transfer (DEPET), capable of the simultaneous study of protein structure and function. An alternative to FRET-based methods, DEPET is based on the quenching of small conjugated fluorophores by photoinduced electron transfer: a reaction that requires contact of the excited fluorophore with a suitable electron donor. This property allows DEPET to exhibit exceptional spatial and temporal resolution capabilities in the range pertinent to protein conformational change. We report the first implementation of DEPET on human large-conductance K+ (BK) channels under voltage clamp. We describe conformational rearrangements underpinning BK channel sensitivity to electrical excitation, in conducting channels expressed in living cells. Finally, we validate DEPET in synthetic peptide length standards, to evaluate its accuracy in measuring sub- and near-nanometer intramolecular distances.