Please use this identifier to cite or link to this item:
http://hdl.handle.net/2445/102162
Title: | Residues coevolution guides the systematic identification of alternative functional conformations in proteins |
Author: | Sfriso, Pedro Duran Frigola, Miquel Mosca, Roberto Emperador, Agustí Aloy, Patrick, 1972- Orozco López, Modesto |
Keywords: | Proteïnes Proteòmica Biologia molecular Proteins Proteomics Molecular biology |
Issue Date: | 10-Dec-2015 |
Publisher: | Elsevier B.V. |
Abstract: | 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. |
Note: | Versió postprint del document publicat a: http://dx.doi.org/10.1016/j.str.2015.10.025 |
It is part of: | Structure, 2016, vol. 24, num. 1, p. 116-126 |
URI: | http://hdl.handle.net/2445/102162 |
Related resource: | http://dx.doi.org/10.1016/j.str.2015.10.025 |
ISSN: | 0969-2126 |
Appears in Collections: | Articles publicats en revistes (Bioquímica i Biomedicina Molecular) Articles publicats en revistes (Institut de Recerca Biomèdica (IRB Barcelona)) Publicacions de projectes de recerca finançats per la UE |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
660509.pdf | 13.29 MB | Adobe PDF | View/Open |
This item is licensed under a Creative Commons License