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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...
Reconstructing the energy landscape of a protein holds the key to characterizing its structural dynamics and function [1]. While the disparate spatio-temporal scales spanned by the slow dynamics challenge reconstruction in wet and dry laboratories, computational efforts have had recent success on proteins where a wealth of experimentally-known structures can be exploited to extract modes of motion...
Proteins are macromolecules in perpetual motion, switching between structural states to modulate their function. A detailed characterization of the precise yet complex relationship between protein structure, dynamics, and function requires elucidating transitions between functionally-relevant states. Doing so challenges both wet and dry laboratories, as protein dynamics involves disparate temporal...
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