The consortium of universities to which the £2.1 million grant has been awarded include the University of Bath, Imperial College London, University of Surrey, Loughborough University, Policy Studies Institute, University of Strathclyde, University of East Anglia, and the University of Leeds.
The project, entitled 'Transition pathways to a low carbon economy', will explore how the UK is to achieve its aim of a low carbon society, including what the future energy mix of the UK might look like.
The £10 million fund is open to all UK universities who wish to research the next generation of low carbon energy solutions.
Professor Matthew Leach, from the Centre for Environmental Strategy at the University of Surrey, comments: “The UK Government has set strong long term targets for tackling climate change, which will require changes in the types of energy technologies installed, in the fuels used and greater efforts at energy efficiency. There is plenty of analysis of what might need to be in place to meet those targets in, say, 2050, but very little understanding of the practical impacts of, and barriers to, the ‘pathways’ that the country needs to follow to get from our current position to a low carbon future. The consortium comprises leading engineers, social scientists and policy analysts who will investigate what changes are needed at all levels of the energy system: from how the large energy utilities might evolve to how householders might be interacting with smart meters and rooftop solar energy.”
The five-year programme of work under the partnership was developed with support from four partner universities that already have expertise in low carbon research – Loughborough University, University of Nottingham, University of Birmingham and Imperial College, London.
Stuart Miller | alfa
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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