|COOKIES: By using this website you agree that we can place Google Analytics Cookies on your device for performance monitoring.|
Enzyme catalysis from linear-scaling DFT: application to chorismate mutase
If you have a question about this talk, please contact Dr. Mike Towler.
Combined quantum mechanics/molecular mechanics (QM/MM) methods, where only the substrate and a few residues are treated quantum mechanically, have become an important tool in computational enzymology. A recent QM/MM study [Org. Biomol. Chem., 9, 157, (2011)] has identied reaction pathways for the chorismate to prephenate rearrangement in solution and catalysed by Chorismate Mutase (CM). However, QM/MM approaches can be limited in accuracy by the empirical nature of classical force fields and from the interface between the QM and MM regions. The density functional theory code, onetep, uniquely combines near-complete basis set accuracy with computational costs that scale linearly with number of atoms, allowing accurate QM descriptions of the enzyme. We present linear-scaling DFT calculations on structures taken from the CM pathways described above, to examine the convergence of activation and reaction energies as the size of the QM region increases to thousands of atoms.
This talk is part of the Electronic Structure Discussion Group series.
This talk is included in these lists:
Note that ex-directory lists are not shown.
Other listsim BCS East Anglia Beyond Profit Enterprise Stream
Other talksGain of the apical complex, and loss of a plastid: organelle function and evolution in apicomplexan and related parasites TBA The roles of arts therapies in secure settings with specific examples from recent music therapy research studies in prisons and high secure forensic settings in China and Europe Learning Markov Networks for Mixed Big Data: Applications to Cancer Genomics Silent Cinema and the Comedy of Birth: An Evening of Shorts (1896–1935) Laughter as a Catalyst for Change