The bacterial chaperonin GroEL is an ATP-regulated molecular machine. It assists misfolded or partially folded proteins to unfold and refold into the correct native structure. The molecule consists of two rings, each composed of seven subunits. A dominant mechanism of motion during this process, which is predicted by the elastic network model, is the concerted counter-rotation of the two rings. This image displays four successive snapshots, viewed from the top, corresponding to successive steps of this allosteric process (see Yang et al., doi:10.1371/journal.pcbi.1000360).
Image Credit: The image was created by Zheng Yang (University of Pittsburgh, United States of America).
Editorial
Ten Simple Rules To Combine Teaching and Research
PLOS Computational Biology: published April 24, 2009 | https://doi.org/10.1371/journal.pcbi.1000358
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Webb Miller and Trey Ideker To Receive Top International Bioinformatics Awards for 2009 from the International Society for Computational Biology
PLOS Computational Biology: published April 24, 2009 | https://doi.org/10.1371/journal.pcbi.1000375
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PLOS Computational Biology: published April 17, 2009 | https://doi.org/10.1371/journal.pcbi.1000361
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