Protease
Findings in protease reported from Case Western Reserve University
Published in Pharma Investments, Ventures and Law Weekly, October 25th, 2009
According to a study from the United States, "The serpins are an unusual class of protease inhibitors which fold to a metastable form and subsequently undergo a massive conformational change to a stable form when they inhibit their target proteases. The driving force for this conformational change has been extensively investigated by site directed mutagenesis, and it has been found that mutations Which stabilize the metastable form frequently result in activity deficiency."
"Here, we employ hydrogen/deuterium exchange to probe the effects of a cavity Filling mutant of alpha(1)AT. The Gly117 -> Phe substitution fills a cavity between the F-helix and the face of...
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