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Cool farm tool water
(2018)
The agricultural sector accounts for 70% of all water consumption and poses great pressure on ground water resources. Therefore, evaluating agricultural water consumption is highly important as it allows supply chain actors to identify practices which are associated with unsustainable water use, which risk depleting current water resources and impacting future production. However, these assessments are often not feasible for crop producers as data, models and experiments are required in order to conduct them. This work introduces a new on-line agricultural water use assessment tool that provides the water footprint and irrigation requirements at field scale based on an enhanced FAO56 approach combined with a global climate, crop and soil databases. This has been included in the Cool Farm Tool - an online tool which already provides metrics for greenhouse gas emissions and biodiversity impacts and therefore allows for a more holistic assessment of environmental sustainability in farming and agricultural supply chains. The model is tested against field scale and state level water footprint data providing good results. The tool provides a practical, reliable way to assess agricultural water use, and offers a means to engage growers and stakeholders in identifying efficient water management practices. (C) 2018 The Authors. Published by Elsevier Ltd.
We used single-molecule FRET in combination with other biophysical methods and molecular simulations to investigate the effect of temperature on the dimensions of unfolded proteins. With singlemolecule FRET, this question can be addressed even under nearnative conditions, where most molecules are folded, allowing us to probe a wide range of denaturant concentrations and temperatures. We find a compaction of the unfolded state of a small cold shock protein with increasing temperature in both the presence and the absence of denaturant, with good agreement between the results from single-molecule FRET and dynamic light scattering. Although dissociation of denaturant from the polypeptide chain with increasing temperature accounts for part of the compaction, the results indicate an important role for additional temperaturedependent interactions within the unfolded chain. The observation of a collapse of a similar extent in the extremely hydrophilic, intrinsically disordered protein prothymosin suggests that the hydrophobic effect is not the sole source of the underlying interactions. Circular dichroism spectroscopy and replica exchange molecular dynamics simulations in explicit water show changes in secondary structure content with increasing temperature and suggest a contribution of intramolecular hydrogen bonding to unfolded state collapse.
The “HPI Future SOC Lab” is a cooperation of the Hasso Plattner Institute (HPI) and industry partners. Its mission is to enable and promote exchange and interaction between the research community and the industry partners.
The HPI Future SOC Lab provides researchers with free of charge access to a complete infrastructure of state of the art hard and software. This infrastructure includes components, which might be too expensive for an ordinary research environment, such as servers with up to 64 cores and 2 TB main memory. The offerings address researchers particularly from but not limited to the areas of computer science and business information systems. Main areas of research include cloud computing, parallelization, and In-Memory technologies.
This technical report presents results of research projects executed in 2017. Selected projects have presented their results on April 25th and November 15th 2017 at the Future SOC Lab Day events.