The Open Middleware Infrastructure Institute UK (OMII-UK) provides software and support on which the UK e-Science community and its international collaborators will be able to build a sustained future. Teams at the Universities of Southampton, Edinburgh and Manchester are putting their expertise to work with the e-Science community in order to provide advanced tools and components which will empower new research in a wide range of disciplines. This activity is a key feature of the UK's e-Science Programme, which held its annual All Hands Meeting in Nottingham last week.
OMII-UK Director Dr Steven Newhouse commented: ‘OMII-UK is very much focused on the user – researchers, developers and providers – and the great thing about launching at the major UK e-Science event was that we were able to gain further insight into everyone’s projects and requirements.’
Dr Newhouse emphasised that OMII-UK provides software, support and sustainability. The OMII-UK web site provides a catalogue with information about software for e-Science, a repository for contributing and downloading software, an easy-to-install software release that provides a proven collection of software components for configurable installation, and documentation, tutorials and training.
Professor Carole Goble, Chair of OMII-UK, added: ‘It is crucial that the wealth of software and know-how generated by the UK e-Science programme and our innovative Scientists is captured and made available to all. OMII-UK is the key means of doing this.’
OMII-UK gives confidence to the user community in adopting e-Science solutions through software support and training, and provides collaborative mechanisms to enable the e-Science community to help itself. It is also engaged with the international community to define, contribute and disseminate best practice and standards. This is being achieved through the engagement of OMII-UK staff in the Open Grid Forum (OGF), GIN (Grid Interoperability Now), EGEE (Enabling Grids for E-Science), OMII-Europe and other community activities.
Joyce Lewis | 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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