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Conformational Dynamics Govern the Free-Energy Landscape of a Membrane-Interacting Protein
[Image: see text] The equilibrium stabilities and the folding rates of membrane-bound proteins are determined by hydrophobic and polar intermolecular contacts with their environment as well as by intramolecular packing and conformational dynamics. The contributions of these factors, however, remain...
| Autores principales: | , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
American Chemical Society
2018
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| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6690567/ https://www.ncbi.nlm.nih.gov/pubmed/31459283 http://dx.doi.org/10.1021/acsomega.8b01609 |