Christopher Ing

I aim to understand the biophysical mechanisms of wild-type and mutant cytochrome c oxidase using all-atom molecular dynamics. I am particularly interested in ion movement and solvation in these proteins.

Research Interests

Under the guidance of Dr. Pierre Nicholas Roy, I calculated properties of small quantum clusters systems at ultra low temperatures. To achieve this I utilized a path integral molecular dynamics sampling method which I assisted in implementing in the Molecular Modelling Toolkit. The simulation of path integral helium about a fixed CO2 impurity is embedded below for a 64 time-slice helium atom,

http://www.youtube.com/watch?v=zziYdYFpOac

In my current research, I am to advance research in the Pomès Lab on the molecular structure and function of cytochrome c oxidase. Cytochrome c oxidase of R. sphaeroides is depicted in the following figure from J. Phys.: Condens. Matter 23 (2011) 234102. Subunit I, which contains the D channel (inset) and the binuclear centre, highlighted in blue. These are the primary regions of importance to electron and proton transport.

The crystallographic structure of subunit A in cytochrome c oxidase is depicted in the following embedded viewer (modern browsers only). Navigate through the annotated regions of the protein with the left and right arrows below.

Publications

BibBase.org: www.bibbase.org/mendeley/b993edf3eb