Marsh D
Max-Planck-Institut für biophysikalische Chemie, Göttingen, Germany.
Cell Mol Life Sci. 2003 Aug;60(8):1575-80. doi: 10.1007/s00018-003-3171-z.
Magnetic resonance results, principally from 2H-nuclear magnetic resonance, indicate that the mean lipid-chain ordering at the surface of transmembrane proteins is comparable to that in fluid lipid bilayers. Principally, it is the requirement for matching the hydrophobic lengths of lipid and protein that modulates the degree of chain ordering at the lipid-protein interface. The distribution of chain order parameters is, nonetheless, broader in the presence of integral proteins than in fluid lipid bi-layers. The chain configurations of the phospholipids that are resolved in crystals of integral membrane proteins display considerable conformational heterogeneity. Chain C-C dihedral angles are, however, not restricted to the energetically allowable trans and gauche rotamers.This indicates that the chains of a given lipid do not have a unique configuration in protein crystals.
磁共振结果，主要来自2H核磁共振，表明跨膜蛋白表面的平均脂链有序性与流体脂质双层中的相当。主要是由于需要匹配脂质和蛋白质的疏水长度，从而调节脂质 - 蛋白质界面处的链有序程度。然而，在存在整合蛋白的情况下，链序参数的分布比在流体脂质双层中更宽。在整合膜蛋白晶体中解析出的磷脂链构型显示出相当大的构象异质性。然而，链的C-C二面角并不局限于能量上允许的反式和顺式旋转异构体。这表明给定脂质的链在蛋白质晶体中没有独特的构型。
