2026-04-04T00:58:47Zhttps://recercat.cat/oai/request

oai:recercat.cat:2445/1021622025-12-04T21:15:31Zcom_2072_1057col_2072_478781col_2072_478908col_2072_478917

00925njm 22002777a 4500 dc Sfriso, Pedro author Duran Frigola, Miquel author Mosca, Roberto author Emperador, Agustí author Aloy, Patrick, 1972- author Orozco López, Modesto author 2016-09-27T08:51:00Z 2016-12-10T23:01:21Z 2015-12-10 2016-09-27T08:51:06Z 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. Proteïnes Proteòmica Biologia molecular Proteins Proteomics Molecular biology Residues coevolution guides the systematic identification of alternative functional conformations in proteins