  The structural dynamics of macromolecules is important for most
microbiological processes, from protein folding to the origins of
neurodegenerative disorders. Noninvasive measurements of these dynamics are
highly challenging. Recently, optical sensors have been shown to allow
noninvasive time-resolved measurements of the dynamic polarizability of
single-molecules. Here we introduce a method to efficiently predict the dynamic
polarizability from the atomic configuration of a given macromolecule. This
provides a means to connect the measured dynamic polarizability to the
underlying structure of the molecule, and therefore to connect temporal
measurements to structural dynamics. To illustrate the methodology we calculate
the change in polarizability as a function of time based on conformations
extracted from molecular dynamics simulations and using different conformations
of motor proteins solved crystalographically. This allows us to quantify the
magnitude of the changes in polarizablity due to thermal and functional
motions.
