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Background The protein energy landscape underscores the inherent nature of proteins as dynamic molecules interconverting between structures with varying energies. Reconstructing a protein’s energy landscape holds the key to characterizing a protein’s equilibrium conformational dynamics and its relationship to function. Many pathogenic mutations in protein sequences alter the equilibrium dynamics that...
Many pathogenic mutations percolate to protein dysfunction by altering dynamics. Reconstructing protein energy landscapes promises to relate dynamics to function but is generally infeasible due to the disparate spatio-temporal scales involved. Recent algorithmic innovation allows reconstructing energy landscapes of medium-size proteins in the presence of sufficient prior wet-laboratory structure data...
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