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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...

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Publicat a:ACS Omega
Autors principals: Frotscher, Erik, Krainer, Georg, Hartmann, Andreas, Schlierf, Michael, Keller, Sandro
Format: Artigo
Idioma:Inglês
Publicat: American Chemical Society 2018
Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC6690567/
https://ncbi.nlm.nih.gov/pubmed/31459283
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acsomega.8b01609
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