Barrera Francisco N, Alcaraz Luis A, Hurtado-Gómez Estefanía, Neira José L
Instituto de Biología Molecular y Celular, Universidad Miguel Hernández, Elche (Alicante), Spain.
Curr Protein Pept Sci. 2008 Dec;9(6):626-37. doi: 10.2174/138920308786733949.
The first comprehensive studies on the structure and thermodynamics of membrane proteins have started revealing the exact architecture of these macromolecules and the physical-chemical rules behind their structures. In this review, the stabilities of several families of membrane proteins, obtained by using spectroscopic, calorimetric and single molecule techniques are surveyed. The data on the stability of membrane proteins are compared with those obtained in soluble proteins. The comparison indicates that although the number of particular atomic interactions is larger in membrane proteins than in soluble ones, the overall values are similar. The consensus is that some intrinsic properties of membrane proteins resemble those of soluble ones, but there are critical differences arising form the inter-molecular contacts with the surrounding membrane. Taken together, all these efforts improve our understanding of the universal forces governing protein folding, and will help in the design of membrane proteins in the near future.
对膜蛋白结构和热力学的首批全面研究已开始揭示这些大分子的确切结构以及其结构背后的物理化学规律。在本综述中，我们调查了通过光谱学、量热法和单分子技术获得的几类膜蛋白的稳定性。将膜蛋白稳定性的数据与可溶性蛋白的数据进行了比较。比较结果表明，尽管膜蛋白中特定原子相互作用的数量比可溶性蛋白中的多，但总体数值相似。普遍的看法是，膜蛋白的一些内在特性与可溶性蛋白的相似，但与周围膜的分子间接触会产生关键差异。综上所述，所有这些努力增进了我们对支配蛋白质折叠的普遍作用力的理解，并将有助于在不久的将来设计膜蛋白。
