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Free energy calculation is critical in predictive tasks such as proteinfolding, docking and design. However, rigorous calculation of free energychange is prohibitively expensive in these practical applications. The minimumpotential energy is therefore widely utilized to approximate free energy. Inthis study, based on analysis of extensive molecular dynamics (MD) simulationtrajectories of a few native globular proteins, we found that change of minimumand corresponding maximum potential energy terms exhibit similar level ofcorrelation with change of free energy. More importantly, we demonstrated thatchange of span (maximum - minimum) of potential energy terms, which engendernegligible additional computational cost, exhibit considerably strongercorrelations with change of free energy than the corresponding change ofminimum and maximum potential energy terms. Therefore, potential energy spanmay serve as an alternative efficient approximate free energy proxy.

Utility of potential energy span as an approximate free energy proxy