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Shape had been intuitively recognized to play a dominant role in determiningthe global motion patterns of bio-molecular assemblies. However, it is notclear exactly how shape determines the motion patterns. What about the localinteractions that hold a structure together to a certain shape? Thecontributions of global shape and local interactions usually mix together andare difficult to tease part. In this work, we use symmetry to elucidate thedistinct roles of global shape and local interactions in protein dynamics.Symmetric complexes provide an ideal platform for this task since in them theeffects of local interactions and global shape are separable, allowing theirdistinct roles to be identified. Our key findings based on symmetric assembliesare: (i) the motion patterns of each subunit are determined primarily byintra-subunit interactions (IRSi), and secondarily by inter-subunitinteractions (IESi); (ii) the motion patterns of the whole assembly are fullydictated by the global symmetry/shape and have nothing to do with local iESi orIRSi. This is followed by a discussion on how the findings may be generalizedto complexes in any shape, with or without symmetry.

Use Symmetry to Elucidate the Roles of Global Shape and Local Interactions in Protein Dynamics and Cooperativity