Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET) and Departamento de Microbiología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Suipacha 531 (S2002LRK) Rosario, Argentina.
Curr Protein Pept Sci. 2011 Dec;12(8):760-6. doi: 10.2174/138920311798841681.
The influence of the lipid environment on the function of membrane proteins is increasingly recognized as crucial. Nevertheless, the molecular mechanisms underlying protein-lipid interactions remain obscure. Membrane lipid composition has a regulatory effect on membrane protein activity, and for a number of membrane proteins a clear correlation was found between protein activity and properties of the membrane bilayer such as fluidity. Membrane thickness is an important property of a lipid bilayer. It is expected that hydrophobic thickness match the hydrophobic thickness of transmembrane segments of integral membrane proteins. Any mismatch between the hydrophobic thicknesses of the lipid bilayer and the protein would lead to some modification in either the structure of the protein or the structure of the bilayer, or both. Consequent rearrangements may result in changes in protein activity. Here we review the behavior of several transmembrane proteins whose activity is altered by hydrophobic core thickness.
脂质环境对膜蛋白功能的影响正日益受到重视。然而，蛋白质-脂质相互作用的分子机制仍不清楚。膜脂组成对膜蛋白活性具有调节作用，对于许多膜蛋白，人们发现其蛋白活性与其膜双层的流动性等特性之间存在明确的相关性。膜厚度是脂质双层的一个重要特性。人们期望疏水区的厚度与整合膜蛋白的跨膜片段的疏水区厚度相匹配。如果脂质双层的疏水区厚度与蛋白质不匹配，那么蛋白质的结构或双层的结构，或者两者都会发生一些改变。随之而来的重新排列可能导致蛋白质活性的改变。在这里，我们回顾了几种跨膜蛋白的行为，它们的活性会被疏水区厚度改变。
