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Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/102162
Residues coevolution guides the systematic identification of alternative functional conformations in proteins
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We present here a new approach for the systematic identification of functionally relevant conformations in proteins. Our fully automated pipeline, based on discrete molecular dynamics enriched with coevolutionary information, is able to capture alternative conformational states in 76% of the proteins studied, providing key atomic details for understanding their function and mechanism of action. We also demonstrate that, given its sampling speed, our method is well suited to explore structural transitions in a high-throughput manner, and can be used to determine functional conformational transitions at the entire proteome level.
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SFRISO, Pedro, et al. Residues coevolution guides the systematic identification of alternative functional conformations in proteins. Structure. 2016. Vol. 24, num. 1, pags. 116-126. ISSN 0969-2126. [consulted: 8 of October of 2026]. Available at: https://hdl.handle.net/2445/102162