Jung-Chi Liao, Research Associate

http://www.stanford.edu/~liaojc/

Myosin converts ATP chemical energy into mechanical work such as muscle contractions, cell division, and vesicle transports. My interests lie in integrating experimental and computational techniques together to understand its mechanochemical energy transduction.

We have developed a computational program, AlloPathFinder, to identify allosteric communication pathways based on conservation analysis. Applying this program to the myosin structures, we identified the allosteric pathways from the ATP-binding site to myosin's lever arm. (JMB, 373:1361-1373, 2007)

We have also developed a computational method to simulate dwell-time distributions of single molecule experiments. Comparing the simulation results with data from single molecule experiments for myosin V, we showed that its power stroke likely occurs after phosphate release and before ADP release. (PNAS, 104:3171-3716, 2007)

Recently, we have designed chimeric myosin VI with artificial lever arms to identify key structural elements of myosin VI dictating its reverse directionality. We implemented computational modeling and molecular dynamics simulation to guide the chimera design. We then used in vitro motility and total internal reflection fluorescence assays to test these chimeras. We found that as few as 18 amino acids are enough to change the myosin directionality. (http://wiki.simtk.org/m6chimera/)