HELICAL AMPHIPATHIC MOMENT - APPLICATION TO PLASMA-LIPOPROTEINS
HELICAL AMPHIPATHIC MOMENT - APPLICATION TO PLASMA-LIPOPROTEINS
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DOI：
10.1016/0014-5793(83)80408-6
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发表时间：
1983-01-01
期刊：
影响因子：
3.5
通讯作者：
MASSEY, JB
中科院分区：
文献类型：
--
作者：
POWNALL, HJ;KNAPP, RD;MASSEY, JB
载脂蛋白与表面的结合是随着α-螺旋的发展而发生的，在该螺旋中形成了极性和非极性的面。螺旋位于脂水界面，极面朝向水相，非极面穿透脂相。这种排列的能量学是通过将氨基酸从水转移到碳氢化合物的自由能向量相加而得到的螺旋两亲性矩来量化的。结果表明，载脂蛋白的平均残基螺旋两亲性矩始终高于跨膜蛋白。
The association of apolipoproteins with surfaces occurs with the development of an α‐helix in which polar and non‐polar faces are formed. The helix locates at the lipid‐water interface with the polar face directed toward the aqueous phase and the non‐polar face penetrating into the lipid phase. The energetics of this arrangement have been quantified by vector addition of the free energies of transfer of amino acids from water to hydrocarbon to give a resultant helical amphipathic moment. It is shown that the mean residue helical amphipathic moments of the apolipoproteins are consistently higher than those of membrane spanning proteins.