This is the first time since 1977 that the Antarctic Treaty Consultative Meeting has been hosted by the UK. The two-week meeting at Edinburgh International Conference Centre addresses the future environmental, policy and legal challenges facing the continent that was designated for peace and science in 1961. Issues for discussion include enhanced scientific collaboration during the forthcoming International Polar Year, sustainable tourism, biological prospecting, and management of the effects of climate change on the Antarctic environment.
The meeting will be opened officially by HRH the Princess Royal. In a keynote address Lord Triesman, Minister for Overseas Territories, says,
‘The importance of Antarctica as a platform for science cannot be underestimated. As the effects of climate change become more evident, it will be to the Antarctic that we must continue to turn for possible answers – both to examine the pre-history of our planet locked up in Antarctic ice, and to monitor the very stability of that ice-sheet. For sea-level rise, when it comes, will partly have its origins in the southern continent.’
British Antarctic Survey (BAS) undertakes as world-class programme of scientific research and plays an influential leadership role in Antarctic affairs. Professor Chris Rapley, Director of British Antarctic Survey, says,
‘The Polar Regions are crucial to the stability of the planet. But while the Antarctic Treaty System ensures scientific cooperation and collaboration in Antarctica, and seeks to protect its environment, it will increasingly have to confront the impacts on the Antarctic of change outside its jurisdiction, raising new issues of global international negotiation. The forthcoming International Polar Year will provide the sound scientific underpinning for such policies and treaties’
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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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