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Energy landscape underlying spontaneous insertion and folding of an alpha-helical transmembrane protein into a bilayer
Membrane protein folding mechanisms and rates are notoriously hard to determine. A recent force spectroscopy study of the folding of an α-helical membrane protein, GlpG, showed that the folded state has a very high kinetic stability and a relatively low thermodynamic stability. Here, we simulate the...
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| I publikationen: | Nat Commun |
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| Huvudupphovsmän: | , , |
| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
Nature Publishing Group UK
2018
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6251876/ https://ncbi.nlm.nih.gov/pubmed/30470737 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41467-018-07320-9 |
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