Our paper describing work in collaboration with the late Klaus Schulten, “Quantitative Characterization of Domain Motions in Molecular Machines” by Suvrajit Maji, Rezvan Shahoei, Klaus Schulten and Joachim Frank, has just been accepted by The Journal of Physical Chemistry Part B — Biophysical Chemistry, Biomaterials, Liquids, and Soft Matter. It will appear in a Special Issue dedicated to the memory of Klaus Schulten.
The work of molecular machines such as the ribosome is accompanied by conformational changes, often characterized by relative motions of their domains. The method we have developed seeks to quantify these motions in a general way, facilitating comparisons of results obtained by different researchers. Typically there are multiple snapshots of a structure in the form of pdb coordinates resulting from flexible fitting of low-resolution density maps, from X-ray crystallography, or from molecular dynamics simulation trajectories. Our objective is to characterize the motion of each domain as a coordinate transformation using moments of inertia tensor, a method we developed earlier. What has been missing until now are ancillary tools that make this task practical, general, and biologically informative. We have provided a comprehensive solution to this task with a set of tools implemented on the VMD platform. These tools address the need for reproducible segmentation of domains, and provide a generalized description of their motions using principal axes of inertia. Although this methodology has been specifically developed for studying ribosome motion, it is applicable to any molecular machine.