期刊
STRUCTURE
卷 24, 期 1, 页码 116-126出版社
CELL PRESS
DOI: 10.1016/j.str.2015.10.025
关键词
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资金
- Spanish FPU grant
- Spanish Ministry of Science [BIO2012-32868, BIO2013-48222]
- Catalan Government [SGR_2014]
- European Research Council [291433, 614944]
- European Research Council (ERC) [291433, 614944] Funding Source: European Research Council (ERC)
- ICREA Funding Source: Custom
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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