Phillips M C, Hauser H, Leslie R B, Oldani D
Biochim Biophys Acta. 1975 Oct 17;406(3):402-14. doi: 10.1016/0005-2736(75)90019-x.
The conformations adopted by beta-casein and the total apoprotein from serum high density lipoprotein when spread at the air-water interface are compared; the monolayer data are consistent with the apoprotein being alpha-helical and the beta-casein being disordered with segments distributed in loops and trains. The penetration of these hydrophobic proteins into phosphatidylcholine monolayers in different physical states was investigated. More protein can penetrate into monolayers when they are in the liquid-expanded state; for penetration at constant total surface area the lateral compressibility of the lipid is an important factor. The charge and conformation of the polar group of the phospholipid does not have a major influence on the interaction. The mixed films of lipid and protein have a mosaic structure; probably the beta-casein is in a compressed state whereas the apoprotein is extended as alpha-helices in the plane of the interface. The chain-length depedences of the interaction of the apoprotein with phosphatidylcholine monolayers and bilayers are different; when the apoprotein binds to bilayers of shorter-chain phosphatidylcholines it alters the shape of the lipid-water interface whereas with monolayers the interface remains planar throughout.
比较了β-酪蛋白和血清高密度脂蛋白中的总脱辅基蛋白在气-水界面铺展时所采取的构象；单分子层数据表明，脱辅基蛋白呈α-螺旋结构，而β-酪蛋白无序，其片段分布成环和链。研究了这些疏水蛋白在不同物理状态下渗透到磷脂酰胆碱单分子层中的情况。当单分子层处于液体扩张状态时，更多的蛋白质能够渗透进去；对于在恒定总表面积下的渗透，脂质的横向压缩性是一个重要因素。磷脂极性基团的电荷和构象对相互作用没有重大影响。脂质和蛋白质的混合膜具有镶嵌结构；可能β-酪蛋白处于压缩状态，而脱辅基蛋白在界面平面内以α-螺旋形式伸展。脱辅基蛋白与磷脂酰胆碱单分子层和双分子层相互作用的链长依赖性不同；当脱辅基蛋白与短链磷脂酰胆碱双分子层结合时，它会改变脂质-水界面的形状，而与单分子层结合时，界面在整个过程中保持平面状。
