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Surface behavior of apolipoprotein A-I and its deletion mutants at model lipoprotein interfaces
Apolipoprotein A-I (apoA-I) has a great conformational flexibility to exist in lipid-free, lipid-poor, and lipid-bound states during lipid metabolism. To address the lipid binding and the dynamic desorption behavior of apoA-I at lipoprotein surfaces, apoA-I, Δ(185-243)apoA-I, and Δ(1-59)(185-243)apo...
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| Hlavní autoři: | , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
The American Society for Biochemistry and Molecular Biology
2014
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3934732/ https://ncbi.nlm.nih.gov/pubmed/24308948 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1194/jlr.M044743 |
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