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SUMMARY:NMR Inspired Perspectives on Enzymology: The Role of Dimer Asymmet
 ry and Protomer Dynamics in Enzyme Catalysis - Prof Scott Prosser\, Univer
 sity of Toronto Mississauga
DTSTART:20180228T140000Z
DTEND:20180228T151500Z
UID:TALK102001@talks.cam.ac.uk
CONTACT:Florian Buhr
DESCRIPTION:It has been estimated that a typical living cell is packed wit
 h between 2 and 4 million proteins per cubic micron. In nature the most co
 mmon oligomeric state of the protein is a dimer\, while the monomer is far
  less common. Many biologists surmise this is simply a consequence of sequ
 estration and packing efficiency in a highly crowded environment. Chemists
  often argue that proteins are probably dimers for reasons of binding and 
 catalytic cooperativity. Physicists are just plain happy to see another ex
 ample of symmetry. Our studies have focused on a homodimeric bacterial enz
 yme\, which exhibits no cooperativity whatsoever. Upon binding of the firs
 t substrate\, the second substrate is excluded from the empty protomer and
  instead\, the empty protomer facilitates key dynamic steps necessary for 
 catalysis. I will discuss recent NMR experiments aimed at identifying func
 tional states of this dynamic homodimer in addition to studies aimed at un
 derstanding substrate inhibition. 
LOCATION:Pfizer Lecture Theatre\, Department of Chemistry
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