Iijima H, Dunbar J B, Marshall G R
Department of Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110.
Proteins. 1987;2(4):330-9. doi: 10.1002/prot.340020408.
Effective van der Waals radii were calibrated in such a way that molecular models built from standard bond lengths and bond angles reproduced the amino acid conformations observed by crystallography in proteins and peptides. The calibrations were based on the comparison of the Ramachandran plots prepared from high-resolution X-ray data of proteins and peptides with the allowed phi, psi torsional angle space for the dipeptide molecular models. The calibrated radii are useful as criteria with which to filter energetically improbable conformations in molecular modeling studies of proteins and peptides.
根据标准键长和键角构建的分子模型能够重现蛋白质和肽中通过晶体学观察到的氨基酸构象。校准基于对从蛋白质和肽的高分辨率X射线数据制备的拉马钱德兰图与二肽分子模型允许的φ、ψ扭转角空间的比较。校准后的半径可作为在蛋白质和肽的分子建模研究中筛选能量上不太可能的构象的标准。
