  A simple force-probe setup is employed to study the mechanical properties of
transcription activator-like effector (TALE) proteins in computer experiments.
It is shown that their spring-like arrangement benefits superelastic behaviour
which is manifested by large-scale global conformational changes along the
helical axis, thus linking structure and dynamics in TALE proteins. As
evidenced from the measured force-extension curves the dHax3 and PthXo1 TALEs
behave like linear springs, obeying Hooke's law, for moderate global structural
changes. For larger deformations, however, the proteins exhibit nonlinearities
and the structures become stiffer the more they are stretched. Flexibility is
not homogeneously distributed over TALE structure, but instead soft spots which
correspond to the RVD loop residues and present key agents in the transmission
of conformational motions are identified.
