Milik M, Skolnick J
Scripps Research Institute, Department of Molecular Biology, La Jolla, California 92037, USA.
Biophys J. 1995 Oct;69(4):1382-6. doi: 10.1016/S0006-3495(95)80007-X.
A Monte Carlo Dynamics simulation was used to investigate the behavior of filamentous bacteriophage coat proteins in a model membrane environment. Our simulation agrees with the previous experimental observations that despite the low sequence similarity between the major coat proteins of Pf1 and fd bacteriophages, their structure in the membrane environment is very similar. These results support the hypothesis that the hydrophobic effect exerts an important influence on membrane protein structure. The model may also be used for modeling the insertion and transport processes in protein-membrane systems. The example of fd protein was also used as a test of sensitivity of our model to temperature, thickness of the hydrocarbon phase, and simulation time. In all cases, the results were independent (over the tested range) of the particular values of the parameters.
采用蒙特卡罗动力学模拟来研究丝状噬菌体外壳蛋白在模型膜环境中的行为。我们的模拟结果与之前的实验观察结果一致，即尽管Pf1和fd噬菌体的主要外壳蛋白之间的序列相似性较低，但它们在膜环境中的结构非常相似。这些结果支持了疏水效应会对膜蛋白结构产生重要影响这一假说。该模型还可用于模拟蛋白质-膜系统中的插入和转运过程。fd蛋白的例子也被用作测试我们的模型对温度、烃相厚度和模拟时间的敏感性。在所有情况下，结果（在所测试的范围内）与参数的具体值无关。
