Energy landscape underlying spontaneous insertion and folding of an alpha-helical transmembrane protein into a bilayer
The detailed folding mechanisms of membrane proteins in their natural bilayer-like environments remains poorly understood due to the lack of tools for measuring stabilities and kinetics. Here, by simulating the folding of GlpG in a bilayer, the authors provide support for the helical-hairpin hypothe...
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| Autores principales: | , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Nature Portfolio
2018
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/3b629c330a4c40749ac3167daefde321 |
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| Sumario: | The detailed folding mechanisms of membrane proteins in their natural bilayer-like environments remains poorly understood due to the lack of tools for measuring stabilities and kinetics. Here, by simulating the folding of GlpG in a bilayer, the authors provide support for the helical-hairpin hypothesis and prompt a re-evaluation of a long-standing paradigm, the two-stage hypothesis. |
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