Instituto Gulbenkian de Ciência, Portugal
Robustness conservation of structural changes of protein assemblies
The function of proteins is determined by changes in their atomic structure. At the same time, biophysical experiments demonstrate that few variables (rotation angles, pulling forces, etc.) can account for dominant features of protein function. However, it is not clear how to connect these dominant features to the atomistic changes. I will present a systematic method to quantify the structural changes of protein assemblies based on finite strain theory. I will apply this method to the case of ATP synthase, and show that, despite prevalent asymmetries, the spatial distribution of deformations is strongly conserved within a synthase. I will further discuss the evolutionary robustness of this conservation. The identification of a deformation-mode that is stable across the tree of life suggests that our method can be used to coarse grain the structural changes of proteins.