Stucture, function and folding of a novel subtilisin serine protease
ISPs constitute the major cellular proteolytic activity of many bacilli, yet their physiological role, mechanism of regulation and 3D structure were unknown. ISP from B. clausii is expressed as a dimeric inactive precursor. Dimerisation is not involved in regulating ISP activity. The 3D structure of...
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Cardiff University
2010
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| Online Access: | http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.584976 |