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Chaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteins
The Escherichia coli chaperonin GroEL is an essential molecular chaperone that mediates protein folding in association with its cofactor, GroES. It is widely accepted that GroEL alternates the GroES-sealed folding-active rings during the reaction cycle. In other words, an asymmetric GroEL–GroES comp...
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| Foilsithe in: | Biophys Physicobiol |
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| Main Authors: | , |
| Formáid: | Artigo |
| Teanga: | Inglês |
| Foilsithe: |
The Biophysical Society of Japan (BSJ)
2016
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| Ábhair: | |
| Rochtain Ar Líne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5042173/ https://ncbi.nlm.nih.gov/pubmed/27924258 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.2142/biophysico.13.0_63 |
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