Based in Germany with local subsidiaries in North America, the UK and Asia-Pacific, Softpro provides biometric solutions that are increasingly used in industries such as banking, insurance, retail, government, health, life sciences and defence. Softpro’s customers include American Express, Bank of America, Barclays, JPMorgan Chase, Lloyds TSB, Saudi Chamber of Commerce and Wachovia.
Its partners include Fujitsu Siemens Computers/Fujitsu, IBM, Microsoft, Motion Computing, Toshiba, Wacom and APP Informatik Davos.
As well as developing its research links with the Department of Electronics, Softpro will fund a prize for the best-performing student on the University’s MSc programme in Information Security and Biometrics.
Professor Michael Fairhurst, Head of the Department of Electronics at Kent and co-founder of the United Kingdom Biometrics Institute (UKBI), said: ‘I am pleased that such an experienced and respected company in international biometric solutions is supporting our MSc programme. The course is already proving to be extremely popular, and it will greatly benefit from Softpro’s support and endorsement.’
Frank Fuchs, CEO of the Softpro Group, added: ‘We highly value the University of Kent’s expertise in biometrics and are happy to support its MSc in Information Security and Biometrics. Softpro is looking forward to continuing its work with Kent on ISO standards and signature-related research projects.’
Kent’s MSc in Information Security and Biometrics provides an advanced level of learning in the field of biometrics and security, providing students with a thorough understanding of the theories, concepts and techniques for the design, development and effective use of secure systems. It also aims to produce graduates who are readily capable of adapting to changes in the field and leading it in innovation.
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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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