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Changes in helical content or net charge of apolipoprotein C-I alter its affinity for lipid/water interfaces
Amphipathic α-helices mediate binding of exchangeable apolipoproteins to lipoproteins. To probe the role of α-helical structure in protein-lipid interactions, we used oil-drop tensiometry to characterize the interfacial behavior of apolipoprotein C-I (apoC-I) variants at triolein/water (TO/W) and 1-...
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| Autores principales: | , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
The American Society for Biochemistry and Molecular Biology
2013
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3679394/ https://ncbi.nlm.nih.gov/pubmed/23670531 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1194/jlr.M037531 |
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