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New research applies algorithms to help explain how homodimeric enzyme breaks one of the strongest chemical bonds found in nature

[ Editor:Public Relations Office  2017 / 2 / 8 Update ]
Recent research findings published by biochemistry groups from University of Toronto together with Adnan Sljoka of Kwansei Gakuin University, who has developed methods and algorithms founded in the area of mathematical rigidity theory with applications to protein structures have shed light on the role of protein dynamics and distant signal propagation (known as “allostery”) as key facets in functional control of an important bacterial enzyme fluoracetate dehalogenase. Their findings appeared in the January 20, 2017 issue of journal Science, in the research article “The role of dimer asymmetry and protomer dynamics in enzyme catalysis” (see full article here http://science.sciencemag.org/content/355/6322/eaag2355).