Proteins aimlessly fluctuate in their functional environments. To robustly achieve activated motions, energy needs to sufficiently flow to the relevant degrees of freedom. Therefore rather than walking on randomly arranged energy landscapes on which different timescales of structural transitions do not have particular order, proteins likely move on hiearchical energy landscapes on which structural life-times play a dominant role. Historically it has been challenging to characterize function related protein energy landscapes, particularly in explicit solvent environments, which has been suggested being an essential part of the landscape. Due to the development of the orthogonal space sampling strategy, hiearchical energy landscapes can be predictively mapped and the results suggest that such landscapes likley dictate protein functional dynamics.

Hierarchical energy landscapes dictate protein functional motions

255th National Meeting (2018)

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