Government publishes UK Marine Science Strategy

By admin on February 5, 2010

The Government has today published a 15 year strategy to deliver world class marine science which will inform decisions on food and energy security, managing the seas sustainably and climate change.

By coordinating marine science across Government, devolved administrations and agencies, the UK will become a world leader in marine environment science and expertise. This partnership approach comes at a time when the need for new knowledge about our oceans and seas has never been greater as we begin to understand the impact that climate change and our own behaviour has had on the Earth’s waters.

The new strategy, a recommendation from the House of Commons Select Committee Report “Investigating the Oceans”, has been developed in partnership with the devolved administrations in Scotland, Wales and Northern Ireland and with significant input from organisations and individuals with marine science interests. It provides a direction for future marine science by identifying three high level priority areas:

• Understanding how the marine ecosystem functions;
• Responding to climate change and its interaction with the marine environment; and
• Sustaining and increasing ecosystem benefits.

Launching the strategy, UK Marine Science Minister, Huw Irranca-Davies, said:
“Our seas and oceans are vital to our very existence, helping to provide us with the air we breathe and supporting eighty per cent of the world’s biodiversity. Seas and oceans also provide us with food and the means to generate renewable energy. Yet the seas and oceans are under pressure from human activities and climate change.

“Understanding how human activities affect the seas and oceans, and how the changes taking place will affect us, is key to making critical policy decisions to enable the marine environment to be managed sustainably. The UK Marine Science Strategy will help to ensure we have the evidence we need to support decisions which will affect generations to come.”

The UK Marine Science Strategy will be delivered through a cross-government committee, reporting to Ministers. This will ensure effective co-ordination of marine science across central government departments, devolved administrations and government agencies. The wider marine science community will also continue to contribute to the strategy and its delivery.

Priority actions that have been identified in a publicly available delivery plan include indentifying gaps in research and developing a more co-ordinated approach to the funding of long-term monitoring of our seas and oceans.

Notes to editors
  1. The UK Marine Science Strategy and associated delivery plan can be found at www.defra.gov.uk/environment/marine/science/mscc.htm and was launched at the Institute of Marine Engineering, Science and Technology.
  2. The strategy was developed by the Marine Science Co-ordination Committee (MSCC) composed of representatives from: Centre for Environment, Fisheries and Aquaculture Science (CEFAS), Department of Business, Innovation and Skills (BIS), Department of Environment, Food and Rural Affairs (Defra) , Department for International Development (DFID), Department for Energy and Climate Change (DECC), Department for Transport (DfT), Environment Agency, Joint Nature Conservation Committee (JNCC), Marine Scotland, Met Office, Ministry of Defence (MoD), Natural Environment Research Council, Northern Ireland Executive, Scottish Environment Protection Agency (SEPA), Scottish Government, Welsh Assembly Government and the United Kingdom Hydrographic Office.  Three independent members also sit on the Committee.
  3. In developing the strategy the MSCC engaged with a wide range of stakeholders with marine science interests through its website and a series of workshops held in London, Reading and Edinburgh.

Reference : http://www.defra.gov.uk/news/2010/100203a.htm

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Teamwork Tackles Larger Protein Structures

By admin on February 5, 2010

ABSTRACT: A protein’s shape determines its function, so this molecular geometry is of extreme interest to scientists and drug companies. But it’s no easy task to deduce a protein’s atomic structure. Now a team has found a way to double the size of a protein that a common technique, called nuclear magnetic resonance (NMR), can decipher.

NMR structuresWorking together. Combining NMR data with computer modeling allows researchers to solve NMR structures of larger proteins. Credit: S. Raman et al., Science

For researchers looking to solve protein structures, the most popular technique remains x-ray crystallography, which bombards crystals of a protein with high-intensity x-rays to reveal their atomic arrangement. Nevertheless, NMR still has two big advantages: It works on proteins that don’t crystallize, and it can reveal a protein’s dynamic nature rather than give a mere static picture.

In a nutshell, NMR works as follows: A solution of a molecule is exposed to a magnetic field. The atomic nuclei (especially hydrogen nuclei) behave like gyroscopes. The precise rate at which a nucleus turns depends on the exact magnetic field at its position, which in turn depends on the relative positions and chemical identities of its neighbors. So from the myriad wobblings, researchers can in principle work out the relative locations of all the nuclei. Given the complexity of analysis, however, NMR has worked best for smaller proteins.

NMR researchers typically collect three kinds of experimental data: an easily acquired set, known as chemical shifts, which depends on what kind of atom the nearest neighbor is; a second set known as residual dipolar coupling (RDC), which is influenced by the orientation of various chemical bonds, and a third method called the Nuclear Overhauser Effect (NOE), which helps to interpret some of the chemical shift data. Interpreting all these data is quite involved.

In 2008, David Baker, a biochemist and protein modeling expert at the University of Washington, Seattle, made a breakthrough in simplifying the task. He and his colleagues did away with the need for the NOE and RDC data by combing chemical shift data into their protein-modeling software called ROSETTA. That allowed them to consistently determine the correct shape of moderate-sized proteins–containing up to 100 amino acids–a feat that had been accomplished only in a hit-or-miss way with early protein-modeling software.

For their current study, Baker and colleagues wanted to see if they could extend their hybrid approach to even larger proteins. To do so, they added back a small amount of the NOE and RDC data, but just in the parts of the analysis that deduce the shape of the general backbone of the protein rather then the position of all the individual atoms in each amino acid side chain. They then relied on their ROSETTA software to sort out the position of the atoms in the protein’s side chains. The team reports online in Science Express that their latest hybrid succeeded in working out the structure of proteins up to 200 amino acids long.

揑t’s a very important development and shows where we are likely to be going as a field,� says Ad Bax, an NMR expert at the National Institute of Diabetes and Digestive and Kidney Diseases in Bethesda, Maryland. Proteins of that size have been solved by NMR before, but only with an amount of time and effort beyond most NMR teams. It’s also a size of many biologically important proteins, such as proteins wedged into cell membranes, which are difficult to crystallize. So Bax notes that as the new hybrid approach matures, it may prove useful in mapping some of these vital proteins for the first time.

Related Site:NMR Structure Determination for Larger Proteins Using Backbone-Only Data

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A polar bear photographed in Arctic Sunrise

By admin on February 3, 2010

a-polar-bearA polar bear photographed from the deck of the Greenpeace ship Arctic Sunrise, in drifting and unconsolidated sea ice in Kane Basin. The bear came within 2 metres of the ship, after moving very fast across the ice towards the bow. Sensing food, it sniffed the air and stayed near the ship for nearly 10 minutes before leaving to hunt a seal in the distance.

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