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In the present study, conservation and covariance properties derived from both sequence and structural dynamics data are integrated with results from Perturbation Response Scanning and in vivo functional assays, so as to establish the dynamical basis of interdomain signal transduction in Hsp70s. We see that the WxxAK motif interacts with I and P, which are also highly conserved indicated by green stars on the left panel , thus forming a tight network of interactions. Those models have revealed the evolutionary conservation of protein flexibility and have given us insights into the slow dynamics required for protein function and mechanistic insight into the allosteric effect. Sequence Evolution Correlates with Structural Dynamics. It is usually considered that the main structural determinant of a site's rate of evolution is its Relative Solvent Accessibility RSA. We suggest that the global conservation of the intrinsic dynamics in the TBF contributes greatly to its success as an enzymic scaffold both through evolution and enzyme design. We present a systematic method of approach for characterizing the sequence, structure, dynamics, and allosteric signaling properties of these enzymes using a combination of structure-based models and methods and bioinformatics tools applied to a data set of 88 structures.

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