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SUMMARY:Enzyme catalysis from linear-scaling DFT: application to chorismat
 e mutase - Greg Lever (TCM)
DTSTART:20120523T104000Z
DTEND:20120523T110000Z
UID:TALK37045@talks.cam.ac.uk
CONTACT:Dr. Mike Towler
DESCRIPTION:Combined quantum mechanics/molecular mechanics (QM/MM) methods
 \, where\nonly the substrate and a few residues are treated quantum\nmecha
 nically\, have become an important tool in computational\nenzymology. A re
 cent QM/MM study [Org. Biomol. Chem.\, 9\, 157\, (2011)]\nhas identied rea
 ction pathways for the chorismate to prephenate\nrearrangement in solution
  and catalysed by Chorismate Mutase (CM).\nHowever\, QM/MM approaches can 
 be limited in accuracy by the empirical\nnature of classical force fields 
 and from the interface between the QM\nand MM regions. The density functio
 nal theory code\, onetep\, uniquely\ncombines near-complete basis set accu
 racy with computational costs\nthat scale linearly with number of atoms\, 
 allowing accurate QM\ndescriptions of the enzyme. We present linear-scalin
 g DFT calculations\non structures taken from the CM pathways described abo
 ve\, to examine\nthe convergence of activation and reaction energies as th
 e size of the\nQM region increases to thousands of atoms.
LOCATION:TCM Seminar Room\, Cavendish Laboratory
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