<title>Author Summary</title> <p>Most proteins are biomolecular machines. They perform their function by undergoing changes between different structures. Understanding the mechanism of transition between these structures is of major importance to design methods for controlling such transitions, and thereby modulating protein function. Although there are many computational methods for exploring the transitions of small proteins, the task of exploring the transition pathways becomes prohibitively expensive in the case of supramolecular systems. The bacterial chaperonin GroEL is such a supramolecular machine. It plays an important role in assisting protein folding. During its function, GroEL undergoes structural transitions between multiple forms. Here, we are introducing a new methodology, based on elastic network models, for elucidating the transition mechanisms in such supramolecular systems. Application to GroEL provides us with biologically significant information on critical interactions and sequence of events occurring during the chaperonin machinery and key contacts that make and break at the transition. The method can be readily applied to other supramolecular machines.</p>
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