Anderson A G, Hermans J
Department of Biochemistry, School of Medicine, University of North Carolina, Chapel Hill 27599-7260.
Proteins. 1988;3(4):262-5. doi: 10.1002/prot.340030408.
A direct attack on the protein-folding problem has been initiated with the free energy perturbation methods of molecular dynamics. The complete conformational probability map for the alanine dipeptide is presented. This work uses the SPC model for the explicit hydration of the dipeptide. Free energy differences for the four observed minima (beta, alpha R, alpha L, C7ax) are given, and the free energy barriers between minima are outlined.
利用分子动力学的自由能微扰方法，已对蛋白质折叠问题展开了直接研究。文中给出了丙氨酸二肽完整的构象概率图。这项研究采用SPC模型对二肽进行显式水合处理。给出了四个观测到的极小值（β、αR、αL、C7ax）的自由能差，并概述了各极小值之间的自由能势垒。
